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Entry version 119 (29 Sep 2021)
Sequence version 2 (10 Jun 2008)
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Protein

Protein adenylyltransferase and cysteine protease IbpA

Gene

ibpA

Organism
Histophilus somni (strain 2336) (Haemophilus somnus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific tyrosine residue of host Rho GTPases RhoA, Rac and Cdc42. The resulting AMPylation inactivates Rho GTPases, thereby inhibiting actin assembly in infected cells. Probably also acts as a cysteine protease, which may play a central role after invasion of host cell and in virulence. Possible member (with IbpB) of a 2 partner secretion. Probably able to bind bovine epithelial cells (host cells). May participate in the formation of fibrils at the surface of the bacteria.

4 Publications

Miscellaneous

The reaction mechanisms probably follows a substrate-assisted attack of ATP. According to this model, His-3717 acts by attracting a proton from the Tyr substrate, thereby preparing the Tyr as a nucleophile to attack the alpha-phosphate of ATP. This model is consistent with the observation that hydrolysis of ATP is very slow in the absence of Rho GTPases (PubMed:20622875).1 Publication

Caution

Was originally [PubMed:8245839] thought to be a 76 kDa immunoglobulin-binding protein; it is now apparent that the gene is much longer but how it is translated and processed is unclear.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei3728ATP1
Binding sitei3757ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3910For cysteine protease activitySequence analysis1
Active sitei4033For cysteine protease activitySequence analysis1
Active sitei4048For cysteine protease activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi3670 – 3671ATP2
Nucleotide bindingi3722 – 3724ATP3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Nucleotidyltransferase, Protease, Thiol protease, Transferase
Biological processVirulence
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
HSOM228400:G1GB8-1552-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein adenylyltransferase and cysteine protease IbpA
Short name:
HMW IgBP
Alternative name(s):
p120
Cleaved into the following chain:
Alternative name(s):
76 kDa antigen
Including the following 2 domains:
Protein adenylyltransferase IbpA (EC:2.7.7.n12 Publications)
Alternative name(s):
AMPylator IbpA
Cysteine protease IbpA (EC:3.4.22.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ibpA
Synonyms:p76
Ordered Locus Names:HSM_1489
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri228400 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008543 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell outer membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3535 – 3536IP → AA: Reduced adenylyltransferase toward Rho GTPase family proteins. 1 Publication2
Mutagenesisi3552 – 3553IL → AA: Reduced adenylyltransferase toward Rho GTPase family proteins. 1 Publication2
Mutagenesisi3668 – 3670LTK → ATA: Reduced adenylyltransferase activity. 1 Publication3
Mutagenesisi3717H → A: Abolishes adenylyltransferase activity. 2 Publications1
Mutagenesisi3723N → A: Does not affect adenylyltransferase activity. 1 Publication1
Mutagenesisi3724G → A: Nucleotide-binding mutant. No adenylyltransferase activity abd reduced toxicity. 1 Publication1
Mutagenesisi3725R → A: Does not affect adenylyltransferase activity. 1 Publication1
Mutagenesisi3728R → A: Does not affect adenylyltransferase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 97Sequence analysisAdd BLAST97
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000033840898 – 4095Protein adenylyltransferase and cysteine protease IbpAAdd BLAST3998
ChainiPRO_00001925103222 – 4095Protein p76 IgBPAdd BLAST874

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The long form of the protein is probably processed, and/or the transcript may be subject to differential translational initiation.

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q06277

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Immunoglobulin-binding protein.

1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

14095
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q06277

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q06277

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati2250 – 22711Add BLAST22
Repeati2272 – 22952Add BLAST24
Repeati2296 – 23173Add BLAST22
Repeati2318 – 23434Add BLAST26
Repeati2344 – 23655Add BLAST22
Repeati2366 – 23876Add BLAST22
Repeati2388 – 24137Add BLAST26
Repeati2414 – 24358Add BLAST22
Repeati2436 – 24579Add BLAST22
Repeati2458 – 248310Add BLAST26
Repeati2484 – 250511Add BLAST22
Repeati2506 – 252712Add BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3218 – 3355Fido 1PROSITE-ProRule annotationAdd BLAST138
Domaini3640 – 3777Fido 2PROSITE-ProRule annotationAdd BLAST138

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni972 – 1515Binds bovine IgG2 FcAdd BLAST544
Regioni1082 – 1117DisorderedSequence analysisAdd BLAST36
Regioni1116 – 1255Binds bovine IgG2 FcAdd BLAST140
Regioni1130 – 1154DisorderedSequence analysisAdd BLAST25
Regioni1204 – 1223DisorderedSequence analysisAdd BLAST20
Regioni1625 – 1652DisorderedSequence analysisAdd BLAST28
Regioni1705 – 1732DisorderedSequence analysisAdd BLAST28
Regioni2250 – 252712 X 22 AA approximate repeatsAdd BLAST278
Regioni2592 – 2617DisorderedSequence analysisAdd BLAST26
Regioni2765 – 2809DisorderedSequence analysisAdd BLAST45
Regioni2825 – 2894DisorderedSequence analysisAdd BLAST70
Regioni2914 – 2933DisorderedSequence analysisAdd BLAST20
Regioni2943 – 3033DisorderedSequence analysisAdd BLAST91
Regioni3049 – 3069DisorderedSequence analysisAdd BLAST21
Regioni3222 – 4095yopT-likeAdd BLAST874
Regioni3354 – 3698Binds bovine IgG2 FcAdd BLAST345
Regioni3357 – 3415DisorderedSequence analysisAdd BLAST59
Regioni3432 – 3454DisorderedSequence analysisAdd BLAST23
Regioni3535 – 3557Arm regionAdd BLAST23
Regioni3783 – 3829DisorderedSequence analysisAdd BLAST47

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1116 – 1247Sequence analysisAdd BLAST132

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1094 – 1117Basic and acidic residuesSequence analysisAdd BLAST24
Compositional biasi1139 – 1153Polar residuesSequence analysisAdd BLAST15
Compositional biasi1636 – 1652Polar residuesSequence analysisAdd BLAST17
Compositional biasi2592 – 2613Polar residuesSequence analysisAdd BLAST22
Compositional biasi2772 – 2803Polar residuesSequence analysisAdd BLAST32
Compositional biasi2977 – 3025Polar residuesSequence analysisAdd BLAST49
Compositional biasi3052 – 3069Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi3361 – 3400Polar residuesSequence analysisAdd BLAST40
Compositional biasi3439 – 3454Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi3783 – 3800Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi3801 – 3829Polar residuesSequence analysisAdd BLAST29

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fido domains mediate the adenylyltransferase activity.
The arm region dictates the ability to recognize Rho family proteins. Leu-3668 and Lys-3670 probably lock the position of Tyr substrate in the correct orientation for modification (PubMed:20622875).1 Publication
When associated with Cdc42 target, adopts a conformation that mimicks the GDI-bound state of Rho GTPases.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the central section; belongs to the fic family.Curated
In the C-terminal section; belongs to the peptidase C58 family.Curated

Keywords - Domaini

Coiled coil, Repeat, Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000190_0_0_6

Identification of Orthologs from Complete Genome Data

More...
OMAi
CETPECQ

Database of Orthologous Groups

More...
OrthoDBi
132791at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3290.10, 2 hits
2.160.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR024973, ESPR
IPR003812, Fido
IPR036597, Fido-like_dom_sf
IPR040198, Fido_containing
IPR008638, Filamn_hemagglutn_N
IPR025157, Hemagglutinin_rpt
IPR038765, Papain-like_cys_pep_sf
IPR012334, Pectin_lyas_fold
IPR011050, Pectin_lyase_fold/virulence
IPR003951, Peptidase_C58
IPR006473, Peptidase_C58_Yopt

The PANTHER Classification System

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PANTHERi
PTHR13504, PTHR13504, 2 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF13018, ESPR, 1 hit
PF02661, Fic, 2 hits
PF13332, Fil_haemagg_2, 1 hit
PF05860, Haemagg_act, 1 hit
PF03543, Peptidase_C58, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01376, BACSURFANTGN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00912, Haemagg_act, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF140931, SSF140931, 2 hits
SSF51126, SSF51126, 1 hit
SSF54001, SSF54001, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01901, adhes_NPXG, 1 hit
TIGR01586, yopT_cys_prot, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51459, FIDO, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q06277-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNKNCYKLIF SKTRGCLVPV AECITSAVDS GSSDSVVVSE KTDEEDRQGS
60 70 80 90 100
IEDYRLSNVC LSVKTFLNPV SSALCLNWKS VSVLLLSMVA APNFAQSAEE
110 120 130 140 150
AAKAEKTPKL TEIQNGNDGI QLETKNQNIG VGAGTTENNH PTKLYKTENN
160 170 180 190 200
VIVIDIAKPN DKGISDNRFQ KFNIPNGAVF KNNKDQQRSE LVGYLEGNKN
210 220 230 240 250
LADKEAKVIL NQVTGSELSQ IKGALEILGT KADLVIANQH GINLNGVQTI
260 270 280 290 300
NAGRFVATTS KLIDPNKMEF DVTQGTVTID VNGFATDNLP YLDIVAKKIE
310 320 330 340 350
QKGTIGNKEK EKNKTSETEI TFIAGKGKIK YNIENDGKTK LEVQKDSNTS
360 370 380 390 400
QPSDKEEVAI TGASTGAMHG KSIKLIVTEQ GAGVKHDGII LSENDIKIES
410 420 430 440 450
NKGDIDLGDK LQAKNEISLN NAKRITIANE ITADKSITIT ADDVKLKNNK
460 470 480 490 500
EASATEEAKL KGKGKLASKK VKVEAKKSLV LDDETKVVAT DLELKSQTLT
510 520 530 540 550
NQGRIYGNKV KIDTDKLVNK KEIYAEDNLD ITTKGKTVTV SVNKDNKRKA
560 570 580 590 600
DVKEETVADL DVGFENTGTI ESKSKAKLTF KDNTSFVSKG NKFIKAKDEL
610 620 630 640 650
TIDAQNVVIS ENDELQTTAR LTINAAGNVV NNGLLASGKT LTINAKQGSI
660 670 680 690 700
YNEKGILGAR EQLTLSAKGN NKETEGNIIN GADSLLHSEG KMELDAENTV
710 720 730 740 750
YNLGNIFAKS DLTVKANELI NDVKLSGSIT KKSPYSVLNR YRRSDIASHG
760 770 780 790 800
WHNNDYRLWI NPIEFEKAEV KVEKAGLIRA EGNFKFEGKK GDNQQDATLT
810 820 830 840 850
NHGVINVKNT FEAQNAKVVN NMKAYQANLL TEFFKQKQDI TFNYQPRARL
860 870 880 890 900
FLSALSGQAE RKFNSLEELF DGLFSEQPIT NSSSYYADNS QAVHLLEEIK
910 920 930 940 950
SPTFQKAMTL VFGANWKNED HKKLSQRWKE FKEKQDAHFD YRPTDKAKIL
960 970 980 990 1000
AQRINGKIDE LKNGSTGGFS ESERITVGQH KFDLSKVEFR SEVNRKENLN
1010 1020 1030 1040 1050
NSNVDLSALS DLLSIPNLFV DNSVQLDKTV DKNIEIDEED EFLLKPHTGE
1060 1070 1080 1090 1100
EPDLLNENEL SENGKFLDKL LGEIGEKTYI REVSDDWERD PDEPDEPDYK
1110 1120 1130 1140 1150
TESRLETRDR FDTLPSEVQD KLRQKFNEYK EKAQQKRQAE ALQAKTKNEQ
1160 1170 1180 1190 1200
LQSDLETGYK EEEKRQAKND LEKQAELQQL DQQEKEKLAK EKELQGKINE
1210 1220 1230 1240 1250
EKQQEALAKQ KQEQQKQADA KAKIEEEKRL EEYRKELAKD HQIEEALSKN
1260 1270 1280 1290 1300
QFLKEVDDTR PKVETDPLYR TKLQYINQDE YFGSKYFLNK VGSSTDAGKK
1310 1320 1330 1340 1350
VAVIGDNYLE HQLITKSIEK KVDNHLALKY QVNDAQLVKK LIDNSYFESK
1360 1370 1380 1390 1400
ELGLKVGEAL TKEQQNQLKQ DIVWYVKANI NNKEVLLPQV YFANKTLRDA
1410 1420 1430 1440 1450
EKFKGLGDAL IRANEINLKT RDVLNSGTIS GKNIDIEAEN KIKNRGDILS
1460 1470 1480 1490 1500
EESTRLVGHK GIDNTARSFV NGNGDVEVQR ASIRTEGHLH LEADEDSDIN
1510 1520 1530 1540 1550
SKGSDIKGKT GFVKARNFNT TDTHRTEHSV EKGRIFSKKG EILGYRKEST
1560 1570 1580 1590 1600
QKAISVGSNT EFDHVHFAIK NDVNQEGSKI KAKVVTGVVQ GDYNTKAGRN
1610 1620 1630 1640 1650
AQQTERYIRL DQEYSSGHIS GAGFTVSHER DSQNGEKTNI GGASSNTGTG
1660 1670 1680 1690 1700
FTLGGSFSET REKETSLTHT NSDLQVDHGI LHVLKKAEIG GVDINKHKFT
1710 1720 1730 1740 1750
GKAVEEDEAK AEQQAKAKAA PDATDNAAQK EEPKFKVLSQ SEVDDLMTEK
1760 1770 1780 1790 1800
SANDLFNKYK KVKEDEGFEL SAKEITSNKQ KDEYHLDSER SVLKFGIETE
1810 1820 1830 1840 1850
GHSAIADAVS HVAKEIVEAQ RGVKQDGTVA LQHISDVANI VTGELVGGSS
1860 1870 1880 1890 1900
KFGFERNYET NKVKETSDIR TKIAGNITLS AHGGNLQLKN VESDANSKLT
1910 1920 1930 1940 1950
LQAKRNVDIL DGETTRESTE RQSRQKFAFG INSGCSVMSG GCNGGVSGSV
1960 1970 1980 1990 2000
DGNESFTTEK SVTHNNSLLR AKNLKIAAGK DLNLISSNIK ADHLDLNIKG
2010 2020 2030 2040 2050
KTNIVSKQDS FDRLYRGFDF SASAGAALSS STLVKGNGSF GAGYTHEVEN
2060 2070 2080 2090 2100
RKLLNQQAGI VANRITGQIK DLDLVAAHFI NKDENSGFRV SGNVTSQQLN
2110 2120 2130 2140 2150
DSHHKDGGSV GVSVGINERG ASSFNVRGGR AEQKHYDAVQ KSVISGINLK
2160 2170 2180 2190 2200
DNNVTGEIVD DLSKAKTVTR DDVYASTQFN FEVADLVELG EKAKSKLQSK
2210 2220 2230 2240 2250
FSKAVNNDAE QPTTTRISSE DVVEMVDNPL YGSNADVRKL RTLDEVGEGY
2260 2270 2280 2290 2300
STLGDQNANK GRKLPNGSDD IYSLLGKVKV SGDEPVYDKV SAEGAYDLLG
2310 2320 2330 2340 2350
DSNANKGRTL RNNSDDLYST VGDANSDISR IRSNVYDEIA AGPYSLLGRT
2360 2370 2380 2390 2400
KAAEEHIYEQ IGEGPYSLLG NGSAVRNRTL GGESNSTYST VGDANSDISR
2410 2420 2430 2440 2450
IRSNVYDEIV AGPYSLLGKP KAAEEHIYEQ IGEGPYSLLG NGSAVRNRTL
2460 2470 2480 2490 2500
GGESDSPYST VGDANSDISR IRSNVYDEIV AGPYSLLGRT KAAEEHIYEQ
2510 2520 2530 2540 2550
IGEGPYSLLG NGSAVRNRTL GGESDSPYSL LGGEGTRNKV LADTIESIYS
2560 2570 2580 2590 2600
TLSRPQASSN LEMVDNPLYD SVRRSASDQL PELPTVRNLL NSDTEAGNGT
2610 2620 2630 2640 2650
YSEITSRTRN ANDPLPPLPN EFRTRLSQGA DLADHVYDTI GSIYSVLSKP
2660 2670 2680 2690 2700
KASSNLEMVD NPLYGSVRRA AGDQLPELPT VKTLLNKVEE VGNEIYSEIT
2710 2720 2730 2740 2750
SKTRSANDPL PALPNFRLTQ EVDTADHIYA DINDVVNRAN KAKRDLPATP
2760 2770 2780 2790 2800
EATPKVAVDG GDYATIGEVS PLQPRASRQQ GSSDYEEIPL PQETAPQKTS
2810 2820 2830 2840 2850
PVKRTSAEGE DGYATIAEVL QPRAAKGQVS DYETIPLDEP SQAAVRTERS
2860 2870 2880 2890 2900
AVEGDYAEIT SPSIQPRSAR GQSGGEEFEP FPSEFSSEPQ SPKRALPAEN
2910 2920 2930 2940 2950
AVVNELGNEL KARLKSKEDQ ANPAKAEVSE PIYATLDKSP EGLARAKAKG
2960 2970 2980 2990 3000
DEAAAANPIV KTRVEDDVAP ELPARPSNLS DSISNETIAE NGQSVALGTP
3010 3020 3030 3040 3050
KSAVAESNRN NNGNQKLQSE GAEGVSPKTK SEDKSWFAKV KDFFFAKSNK
3060 3070 3080 3090 3100
SQAKEAKSEQ ETVSKPNYDS LEDDLNLKNL LALEDKRGSS FEENVLKNPE
3110 3120 3130 3140 3150
FLAEAREIAK KYIPEATIKQ MGNSPEFDEI LTEGAKKVEK RINDALTFKP
3160 3170 3180 3190 3200
SVDEFNEIQG LVKNIQKGSA VDDLNAQTLA ITEALADTSK TIQRNPKLKE
3210 3220 3230 3240 3250
EVQGAIEEFL KSSQGKELTV EMIEKLNHGL RPDEGSDRLL YKKENLTKEN
3260 3270 3280 3290 3300
AVFSSPQASK IQLNETVDFI NQAIKQNVEP SVLAGLVYQR LIAYHPFAEG
3310 3320 3330 3340 3350
NGRMARVVVN KILLDAGYPP FTKFSSEFET QIIPQTKATA KSATSAEVVK
3360 3370 3380 3390 3400
EFLTELGKKS SPQEGGANNQ NGQATSPVTL KSKDVSEVEN TQSADSLTIK
3410 3420 3430 3440 3450
QPEQGKAGGQ LPSVPKVETS VNEVAPLSSV PAELKDAAGG NKKAAEKSEG
3460 3470 3480 3490 3500
ATGVEKEKTT LFQRVKQFFT GSKSGAKPVA GDETANKVNY QDLEDNLNLK
3510 3520 3530 3540 3550
GLISLEDDRN ANFESNVLKN EKFLDEAREI SKKSIPEATV KQMSHLPEFD
3560 3570 3580 3590 3600
DILTEGAKKV ESRINKAITF RPSVEEFSEI QDLVKTLPKT KVIEDLSTKT
3610 3620 3630 3640 3650
NEITEALAAT SKTIQRTPEL KEQLKTAIED FLQNSQGKPL TVQMIENLNH
3660 3670 3680 3690 3700
GLRPDEGEGR LLYKKENLTK ENAVFSSPEA AKIQLAETVD FINRAKNEGI
3710 3720 3730 3740 3750
EPSVVGALVY QRLIAYHPFA EGNGRMARVI VNKILLDAGY PAFTKFSDEF
3760 3770 3780 3790 3800
EPQIIPQTKA STKSATSSEV VVEFLKELAK KGSKEDNEQN LEKTDRTSTD
3810 3820 3830 3840 3850
LTESAVENSA ALSSGTVRSA TVSETVTETE QAKAKPVSDL VSSKDLVEQQ
3860 3870 3880 3890 3900
RTVLQRIQDQ FQPLKVKSKI DAVRSSVEEF GGEVSFKFAQ SKGEVYKEIV
3910 3920 3930 3940 3950
KHIETQNGVC ESTCAHWIAK NVNPTDENFF NTLYEGGKKG HLKKETIDSI
3960 3970 3980 3990 4000
KKLQTEFINS GSATQQFKLT DSWLQEQGVV PKEKKVADFV RRDEVSGTVS
4010 4020 4030 4040 4050
KNDVSSLVKA ILDTGDDTAG VKKISINLEG GSHTVSAAVD GSKVTFFDPN
4060 4070 4080 4090
FGEMTFPTHQ QFENWLKNAF WQKSGYAGKQ EGRRFFNVVN YKKNN
Length:4,095
Mass (Da):450,060
Last modified:June 10, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i495723E626D5E7DD
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC36827 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB087258 Genomic DNA Translation: BAC78649.1
L10282 Unassigned DNA Translation: AAC36827.1 Different initiation.
CP000947 Genomic DNA Translation: ACA31239.1

NCBI Reference Sequences

More...
RefSeqi
WP_012340627.1, NC_010519.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ACA31239; ACA31239; HSM_1489

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsm:HSM_1489

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087258 Genomic DNA Translation: BAC78649.1
L10282 Unassigned DNA Translation: AAC36827.1 Different initiation.
CP000947 Genomic DNA Translation: ACA31239.1
RefSeqiWP_012340627.1, NC_010519.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N3UX-ray1.85A3488-3786[»]
4ITRX-ray2.30A/B3482-3797[»]
6SIUX-ray2.49A/B3483-3797[»]
SMRiQ06277
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiQ06277

Genome annotation databases

EnsemblBacteriaiACA31239; ACA31239; HSM_1489
KEGGihsm:HSM_1489

Phylogenomic databases

HOGENOMiCLU_000190_0_0_6
OMAiCETPECQ
OrthoDBi132791at2

Enzyme and pathway databases

BioCyciHSOM228400:G1GB8-1552-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ06277

Family and domain databases

Gene3Di1.10.3290.10, 2 hits
2.160.20.10, 1 hit
InterProiView protein in InterPro
IPR024973, ESPR
IPR003812, Fido
IPR036597, Fido-like_dom_sf
IPR040198, Fido_containing
IPR008638, Filamn_hemagglutn_N
IPR025157, Hemagglutinin_rpt
IPR038765, Papain-like_cys_pep_sf
IPR012334, Pectin_lyas_fold
IPR011050, Pectin_lyase_fold/virulence
IPR003951, Peptidase_C58
IPR006473, Peptidase_C58_Yopt
PANTHERiPTHR13504, PTHR13504, 2 hits
PfamiView protein in Pfam
PF13018, ESPR, 1 hit
PF02661, Fic, 2 hits
PF13332, Fil_haemagg_2, 1 hit
PF05860, Haemagg_act, 1 hit
PF03543, Peptidase_C58, 1 hit
PRINTSiPR01376, BACSURFANTGN
SMARTiView protein in SMART
SM00912, Haemagg_act, 1 hit
SUPFAMiSSF140931, SSF140931, 2 hits
SSF51126, SSF51126, 1 hit
SSF54001, SSF54001, 1 hit
TIGRFAMsiTIGR01901, adhes_NPXG, 1 hit
TIGR01586, yopT_cys_prot, 1 hit
PROSITEiView protein in PROSITE
PS51459, FIDO, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIBPA_HISS2
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q06277
Secondary accession number(s): B0UUL0, Q7WZI3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 10, 2008
Last modified: September 29, 2021
This is version 119 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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