Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-hemolysin translocation ATP-binding protein HlyB

Gene

hlyB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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_00000923731 – 707Alpha-hemolysin translocation ATP-binding protein HlyBAdd BLAST707

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 20Combined sources12
Helixi27 – 33Combined sources7
Helixi43 – 51Combined sources9
Turni52 – 54Combined sources3
Beta strandi55 – 61Combined sources7
Helixi64 – 67Combined sources4
Beta strandi70 – 76Combined sources7
Beta strandi84 – 89Combined sources6
Turni91 – 93Combined sources3
Beta strandi94 – 100Combined sources7
Turni101 – 104Combined sources4
Beta strandi105 – 110Combined sources6
Helixi111 – 117Combined sources7
Beta strandi120 – 129Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZUANMR-A2-137[»]
ProteinModelPortaliQ47258.
SMRiQ47258.
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.

Q47258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA
60 70 80 90 100
KSLELKVKQV KKTIDRLNFI SLPALVWRED GRHFILTKVS KEANRYLIFD
110 120 130 140 150
LEQRNPRVLE QSEFEALYQG HIILIASRSS VAGKLAKFDF TWFIPAIIKY
160 170 180 190 200
RRIFIETLVV 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 EHIIMRNMHK
660 670 680 690 700
ICKGRTVIII AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY

LYQLQSD
Length:707
Mass (Da):79,529
Last modified:November 1, 1996 - v1
Checksum:iE709E59F21BDA853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81823 Genomic DNA. Translation: AAA23978.1.
PIRiA42255. LEECB.
RefSeqiWP_000376543.1. NZ_NCSC01000001.1.

Similar proteinsi

Entry informationi

Entry nameiHLYB3_ECOLX
AccessioniPrimary (citable) accession number: Q47258
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: July 5, 2017
This is version 101 of the entry and version 1 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

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families