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Entry version 42 (11 Dec 2019)
Sequence version 1 (18 Apr 2012)
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Protein

Protein glycosylation K

Gene

pglK

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
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

Mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. Transport across the membrane is effected via ATP-driven conformation changes. Most likely, only the polar and charged part of the glycolipid enter the substrate-binding cavity, and the lipid tail remains exposed to the membrane lipids during the transmembrane flipping process.3 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

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 bindingi382 – 389ATPPROSITE-ProRule annotation8

<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 functionTranslocase
Biological processTransport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
CJEJ192222:G1G1F-1089-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00378

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.1.106.15 the atp-binding cassette (abc) superfamily

<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 glycosylation K (EC:7.5.2.52 Publications)
<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:pglK
Synonyms:wlaB
Ordered Locus Names:Cj1130c
<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>OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
<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 identifieri192222 [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 lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
<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
  • UP000000799 <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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 15Cytoplasmic1 PublicationAdd BLAST15
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei16 – 38HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST23
Topological domaini39 – 76Extracellular1 PublicationAdd BLAST38
Transmembranei77 – 98HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST22
Topological domaini99 – 149Cytoplasmic1 PublicationAdd BLAST51
Transmembranei150 – 170HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST21
Topological domaini171 – 173Extracellular1 Publication3
Transmembranei174 – 197HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST24
Topological domaini198 – 254Cytoplasmic1 PublicationAdd BLAST57
Transmembranei255 – 276HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST22
Topological domaini277 – 292Extracellular1 PublicationAdd BLAST16
Transmembranei293 – 314HelicalPROSITE-ProRule annotation1 PublicationAdd BLAST22
Topological domaini315 – 564Cytoplasmic1 PublicationAdd BLAST250

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Hypoglycosylation phenotype.1 Publication

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>Mutagenesisi46 – 67SDFSY…YLNIP → GSSGSSGS: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding. Abolishes translocation of lipid-linked oligosaccharide. 1 PublicationAdd BLAST22
Mutagenesisi50Y → A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-56 and A-63. 1 Publication1
Mutagenesisi53 – 55RNK → ANA: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding. Strongly decreases translocation of lipid-linked oligosaccharide. 1 Publication3
Mutagenesisi56Y → A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-50 and A-63. 1 Publication1
Mutagenesisi63Y → A: Abolishes stimulation of ATPase activity by lipid-linked oligosaccharide binding and decreases translocation of lipid-linked oligosaccharide; when associated with A-50 and A-56. 1 Publication1
Mutagenesisi86R → A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-260; A-302 and A-309. 1 Publication1
Mutagenesisi260R → A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-302 and A-309. 1 Publication1
Mutagenesisi302R → A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-260 and A-309. 1 Publication1
Mutagenesisi309R → A: Abolishes translocation of lipid-linked oligosaccharide; when associated with A-86; A-260 and A-302. 1 Publication1
Mutagenesisi388K → A: Reduced efficiency of the N-linked protein glycosylation pathway. 1 Publication1
Mutagenesisi389S → A: Impaired N-linked protein glycosylation pathway. 1 Publication1
Mutagenesisi488G → D: Impaired N-linked protein glycosylation pathway. 1 Publication1
Mutagenesisi492R → C: No effect on the N-linked protein glycosylation pathway. 1 Publication1
Mutagenesisi506L → A: Reduced efficiency of the N-linked protein glycosylation pathway. 1 Publication1
Mutagenesisi510E → Q: Abolishes ATPase activity and strongly reduces translocation of lipid-linked oligosaccharide. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004225841 – 564Protein glycosylation KAdd BLAST564

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q0P9C4

PRoteomics IDEntifications database

More...
PRIDEi
Q0P9C4

<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

Homodimer; domain-swapped. Helices that arise in transmembrane regions 4 and 5 from one subunit cross over and contact the nucleotide-binding domain from the other subunit.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
192222.Cj1130c

<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

3D structure databases

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

More...
SMRi
Q0P9C4

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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 <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>Domaini17 – 319ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST303
Domaini349 – 564ABC transporterPROSITE-ProRule annotationAdd BLAST216

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>Regioni46 – 67Important for stimulation of ATPase activity by lipid-linked oligosaccharides and subsequent translocation of lipid-linked oligosaccharides1 PublicationAdd BLAST22

<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

In the absence of ligand, the homodimer has a V-shaped structure with a large cavity that is accessible from the cytoplasmic side.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

Belongs to the ABC transporter superfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105BZ1 Bacteria
COG1132 LUCA

KEGG Orthology (KO)

More...
KOi
K06148

Identification of Orthologs from Complete Genome Data

More...
OMAi
YRMLPAF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1560.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR011527 ABC1_TM_dom
IPR036640 ABC1_TM_sf
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR027417 P-loop_NTPase
IPR039421 Type_I_exporter

The PANTHER Classification System

More...
PANTHERi
PTHR24221 PTHR24221, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00664 ABC_membrane, 1 hit
PF00005 ABC_tran, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit
SSF90123 SSF90123, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50929 ABC_TM1F, 1 hit
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit

<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.

Q0P9C4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKKLFFILS KEDKNFLFFL LVFSVFISFI ETFAISLVMP FITLASDFSY
60 70 80 90 100
FDRNKYLISL KEYLNIPVFE IIVYFGVGLI VFYVFRALLN AYYFHLLARF
110 120 130 140 150
SKGRYHAIAY KVFSKFLNIN YEKFTQKNQS EILKSITGEV YNLSTMISSF
160 170 180 190 200
LLLMSEIFVV LLLYALMLLI NYKITLFLSI FMVLNAFILV KILSPIIKKA
210 220 230 240 250
GVRREEAMKN FFEILNTNLN NFKFIKLKTK EDGVLSLFKA QSEAFSKANI
260 270 280 290 300
TNESVAAVPR IYLEGIGFCV LVFIVVFLVL KNESDISGIL STISIFVLAL
310 320 330 340 350
YRLMPSANRI ITSYHDLLYY HSSLDIIYQN LRQEEENLGE EKLSFNQELK
360 370 380 390 400
ICNLSFGYEG KKYLFKNLNL NIKKGEKIAF IGESGCGKST LVDLIIGLLK
410 420 430 440 450
PKEGQILIDE QELNANNTKN YRQKIGYIPQ NIYLFNDSIA KNITFGDAVD
460 470 480 490 500
EEKLNRVIKQ ANLEHFIKNL PQGVQTKVGD GGSNLSGGQK QRIAIARALY
510 520 530 540 550
LEPEMLVLDE ATSALDTQSE AKIMDEIYKI SKDKTMIIIA HRLSTITQCD
560
KVYRLEHGKL KEEK
Length:564
Mass (Da):64,739
Last modified:April 18, 2012 - v1
<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:i00C8D00B231EACF3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AL111168 Genomic DNA Translation: CAL35247.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E81317

NCBI Reference Sequences

More...
RefSeqi
WP_002858308.1, NC_002163.1
YP_002344523.1, NC_002163.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAL35247; CAL35247; Cj1130c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
905421

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cje:Cj1130c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|192222.6.peg.1112

<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
AL111168 Genomic DNA Translation: CAL35247.1
PIRiE81317
RefSeqiWP_002858308.1, NC_002163.1
YP_002344523.1, NC_002163.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5C73X-ray5.90A/B/C/F/G/K1-564[»]
5C76X-ray3.94A/B/C/D1-564[»]
5C78X-ray2.90A/B/C/D1-564[»]
5NBDX-ray3.90A/B1-564[»]
SMRiQ0P9C4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi192222.Cj1130c

Protein family/group databases

TCDBi3.A.1.106.15 the atp-binding cassette (abc) superfamily

Proteomic databases

PaxDbiQ0P9C4
PRIDEiQ0P9C4

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
Q0P9C4

Genome annotation databases

EnsemblBacteriaiCAL35247; CAL35247; Cj1130c
GeneIDi905421
KEGGicje:Cj1130c
PATRICifig|192222.6.peg.1112

Phylogenomic databases

eggNOGiENOG4105BZ1 Bacteria
COG1132 LUCA
KOiK06148
OMAiYRMLPAF

Enzyme and pathway databases

UniPathwayiUPA00378
BioCyciCJEJ192222:G1G1F-1089-MONOMER

Family and domain databases

Gene3Di1.20.1560.10, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR011527 ABC1_TM_dom
IPR036640 ABC1_TM_sf
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR027417 P-loop_NTPase
IPR039421 Type_I_exporter
PANTHERiPTHR24221 PTHR24221, 1 hit
PfamiView protein in Pfam
PF00664 ABC_membrane, 1 hit
PF00005 ABC_tran, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF90123 SSF90123, 1 hit
PROSITEiView protein in PROSITE
PS50929 ABC_TM1F, 1 hit
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiPGLK_CAMJE
<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: Q0P9C4
<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: May 29, 2013
Last sequence update: April 18, 2012
Last modified: December 11, 2019
This is version 42 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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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