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Protein

Alpha-hemolysin translocation ATP-binding protein HlyB

Gene

hlyB

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).By similarity

Miscellaneous

The complex HlyBD-TolC (OMF) forms a single transport channel across the two membranes, allowing direct export of alpha-hemolysin. These channel is involved in type 1 secretion system (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei83PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi502 – 509ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processTransport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-hemolysin translocation ATP-binding protein HlyB
Alternative name(s):
EHEC-HlyB protein
Gene namesi
Name:hlyB
Ordered Locus Names:L7049, ECO57PM18
Encoded oniPlasmid pO1570 Publication
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Plasmid pO157
  • UP000002519 Componenti: Plasmid pO157

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei153 – 173HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei191 – 211HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei269 – 289HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei295 – 315HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei388 – 408HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000923751 – 706Alpha-hemolysin translocation ATP-binding protein HlyBAdd BLAST706

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi155864.L7049.

Structurei

3D structure databases

ProteinModelPortaliQ46717.
SMRiQ46717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 125Peptidase C39PROSITE-ProRule annotationAdd BLAST125
Domaini154 – 436ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST283
Domaini468 – 703ABC transporterPROSITE-ProRule annotationAdd BLAST236

Domaini

In HlyB the peptidase C39 domain, the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108JJA. Bacteria.
COG2274. LUCA.
KOiK11004.

Family and domain databases

InterProiView protein in InterPro
IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR010132. ATPase_T1SS_HlyB.
IPR027417. P-loop_NTPase.
IPR005074. Peptidase_C39.
PfamiView protein in Pfam
PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
PF03412. Peptidase_C39. 1 hit.
SMARTiView protein in SMART
SM00382. AAA. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR01846. type_I_sec_HlyB. 1 hit.
PROSITEiView protein in PROSITE
PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS50990. PEPTIDASE_C39. 1 hit.

Sequencei

Sequence statusi: Complete.

Q46717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSKCSSHNS LYALILLAQY HNITVNAETI RHQYNTHTQD FGVTEWLLAA
60 70 80 90 100
KSIGLKAKYV EKHFSRLSII SLPALIWRDD GKHYILSRIT KDSSRYLVYD
110 120 130 140 150
PEQHQSLTFS RDEFEKLYQG KVILVTSRAT VVGELAKFDF SWFIPSVVKY
160 170 180 190 200
RRILLEVLTV SAFIQFLALI TPLFFQVVMD KVLVHRGFST LNIITIAFII
210 220 230 240 250
VILFEVILTG ARTYIFSHTT SRIDVELGAK LFRHLLALPV SYFENRRVGE
260 270 280 290 300
TVARVRELEQ IRNFLTGQAL TSVLDLFFSV IFFCVMWYYS PQLTLVILLS
310 320 330 340 350
LPCYVIWSLF ISPLLRRRLD DKFLRNAENQ AFLVETVTAI NTIKSMAVSP
360 370 380 390 400
QMIATWDKQL AGYVASSFRV NLVAMTGQQG IQLIQKSVMV ISLWMGAHLV
410 420 430 440 450
ISGEISIGQL IAFNMLAGQV IAPVIRLAHL WQDFQQVGIS VERLGDVLNT
460 470 480 490 500
PVEKKSGRNI LPEIQGDIEF KNVRFRYSSD GNVILNNINL YISKGDVIGI
510 520 530 540 550
VGRSGSGKST LTKLLQRFYI PETGQILIDG HDLSLADPEW LRRQIGVVLQ
560 570 580 590 600
ENILLNRSII DNITLASPAV SMEQAIEAAR LAGAHDFIRE LKEGYNTIVG
610 620 630 640 650
EQGVGLSGGQ RQRIAIARAL VTNPRILIFD EATSALDYES ENIIMKNMSR
660 670 680 690 700
ICKNRTVIII AHRLSTVKNA NRIIVMDNGF ISEDGTHKEL ISKKDSLYAY

LYQLQA
Length:706
Mass (Da):79,815
Last modified:May 1, 1999 - v2
Checksum:i9A3C6EB2C2A981EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti259E → D in CAA60043 (PubMed:8936317).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86087 Genomic DNA. Translation: CAA60043.1.
AF074613 Genomic DNA. Translation: AAC70117.1.
AB011549 Genomic DNA. Translation: BAA31775.1.
U12572 Genomic DNA. Translation: AAA20545.2.
PIRiT00228.
RefSeqiNP_052625.1. NC_002128.1.
WP_000987091.1. NZ_LKAL01000035.1.

Genome annotation databases

EnsemblBacteriaiAAC70117; AAC70117; Z_L7049.
BAA31775; BAA31775; BAA31775.
GeneIDi1789727.
KEGGiece:Z_L7049.
ecs:pO157p19.
PATRICifig|386585.9.peg.22.

Similar proteinsi

Entry informationi

Entry nameiHLYB_ECO57
AccessioniPrimary (citable) accession number: Q46717
Secondary accession number(s): Q47462, Q79D74, Q7BSV0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 1999
Last modified: June 7, 2017
This is version 118 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Asn-9 is present instead of the conserved Cys which is expected to be the active site residue of peptidase C39. Thus they are presumed to be without peptidase activity.Curated

Keywords - Technical termi

Complete proteome, Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families