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Protein

Alpha-hemolysin translocation ATP-binding protein HlyB

Gene

hlyB

Organism
Escherichia coli
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
Gene namesi
Name:hlyB
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei158 – 178HelicalPROSITE-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_00000923721 – 707Alpha-hemolysin translocation ATP-binding protein HlyBAdd BLAST707

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-16931N.

Structurei

3D structure databases

ProteinModelPortaliP10089.
SMRiP10089.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 125Peptidase C39PROSITE-ProRule annotationAdd BLAST123
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.

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.

P10089-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA
60 70 80 90 100
KSLELKVKQV KKTIDRLNFI SLPALVWRED GCHFILTKVS KEANRYLIFD
110 120 130 140 150
LEQRNPRVLE QSEFEALYQG HIILIASRSS VTGKLAKFDF TWFIPAIIKY
160 170 180 190 200
RKIFIETLVV SVFLQLFALI TPLFFQVVMD KVLVHRGFST LNVITVALSV
210 220 230 240 250
VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI SYFESRRVGD
260 270 280 290 300
TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS
310 320 330 340 350
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP
360 370 380 390 400
QMTNIWDKQL AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV
410 420 430 440 450
ISGDLSIGQL IAFNMLAGQI VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS
460 470 480 490 500
PTESYHGKLA LPEINGDITF RNIRFRYKPD SPVILDNINL SIKQGEVIGI
510 520 530 540 550
VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW LRRQVGVVLQ
560 570 580 590 600
DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG
610 620 630 640 650
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHVIMRNMHK
660 670 680 690 700
ICKGRTVIII AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY

LYQLQSD
Length:707
Mass (Da):79,464
Last modified:November 1, 1995 - v2
Checksum:i21009CB45E59437E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10133 Genomic DNA. Translation: AAA23976.1.
RefSeqiWP_021525012.1. NZ_JSGE01000112.1.

Similar proteinsi

Entry informationi

Entry nameiHLYBC_ECOLX
AccessioniPrimary (citable) accession number: P10089
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: July 5, 2017
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Tyr-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

Documents

  1. SIMILARITY comments
    Index of protein domains and families