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Protein

Alpha-hemolysin translocation ATP-binding protein HlyB

Gene

hlyB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei83 – 831PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi502 – 5098ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Protein family/group databases

TCDBi3.A.1.109.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-hemolysin translocation ATP-binding protein HlyB
Gene namesi
Name:hlyB
Encoded oniPlasmid IncI2 pHLY1520 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei158 – 17821HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei191 – 21121HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei269 – 28921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei295 – 31521HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei388 – 40821HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707707Alpha-hemolysin translocation ATP-binding protein HlyBPRO_0000092371Add
BLAST

Proteomic databases

PRIDEiP08716.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-28120N.
STRINGi199310.c3573.

Structurei

Secondary structure

1
707
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi467 – 47812Combined sources
Beta strandi483 – 49311Combined sources
Beta strandi497 – 5015Combined sources
Helixi508 – 5158Combined sources
Beta strandi522 – 5287Combined sources
Turni533 – 5353Combined sources
Helixi538 – 5447Combined sources
Beta strandi545 – 5484Combined sources
Beta strandi556 – 5583Combined sources
Helixi559 – 5635Combined sources
Turni564 – 5663Combined sources
Helixi572 – 58110Combined sources
Helixi585 – 5895Combined sources
Beta strandi591 – 5933Combined sources
Helixi594 – 5963Combined sources
Beta strandi598 – 6003Combined sources
Turni601 – 6033Combined sources
Helixi608 – 62013Combined sources
Beta strandi625 – 6295Combined sources
Turni632 – 6354Combined sources
Helixi638 – 65215Combined sources
Beta strandi655 – 6606Combined sources
Helixi664 – 6674Combined sources
Beta strandi670 – 6778Combined sources
Beta strandi680 – 6856Combined sources
Helixi687 – 6915Combined sources
Helixi697 – 7059Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT0X-ray2.60A467-707[»]
1XEFX-ray2.50A/B/C/D467-707[»]
2FF7X-ray1.60A467-707[»]
2FFAX-ray1.70A467-707[»]
2FFBX-ray1.90A467-707[»]
2FGJX-ray2.60A/B/C/D467-707[»]
2FGKX-ray2.70A/B/C/D467-707[»]
2PMKX-ray1.60A467-707[»]
3B5JX-ray2.00A467-707[»]
ProteinModelPortaliP08716.
SMRiP08716. Positions 467-707.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08716.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 125123Peptidase C39PROSITE-ProRule annotationAdd
BLAST
Domaini154 – 436283ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST
Domaini468 – 703236ABC transporterPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
Contains 1 ABC transporter domain.PROSITE-ProRule annotation
Contains 1 peptidase C39 domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108JJA. Bacteria.
COG2274. LUCA.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
PF03412. Peptidase_C39. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR01846. type_I_sec_HlyB. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS50990. PEPTIDASE_C39. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA
60 70 80 90 100
KSLELKVKQV KKTIDRLNFI FLPALVWRED GRHFILTKIS KEVNRYLIFD
110 120 130 140 150
LEQRNPRVLE QSEFEALYQG HIILITSRSS VTGKLAKFDF 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 TSVLDLLFSL 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
PTESYHGKLT 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):79,673
Last modified:January 1, 1988 - v1
Checksum:i412A3EB64A3CFFBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14107 Genomic DNA. Translation: AAA98234.1.
PIRiS10057.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14107 Genomic DNA. Translation: AAA98234.1.
PIRiS10057.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT0X-ray2.60A467-707[»]
1XEFX-ray2.50A/B/C/D467-707[»]
2FF7X-ray1.60A467-707[»]
2FFAX-ray1.70A467-707[»]
2FFBX-ray1.90A467-707[»]
2FGJX-ray2.60A/B/C/D467-707[»]
2FGKX-ray2.70A/B/C/D467-707[»]
2PMKX-ray1.60A467-707[»]
3B5JX-ray2.00A467-707[»]
ProteinModelPortaliP08716.
SMRiP08716. Positions 467-707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-28120N.
STRINGi199310.c3573.

Protein family/group databases

TCDBi3.A.1.109.1. the atp-binding cassette (abc) superfamily.

Proteomic databases

PRIDEiP08716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108JJA. Bacteria.
COG2274. LUCA.

Miscellaneous databases

EvolutionaryTraceiP08716.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. 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.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
PF03412. Peptidase_C39. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsiTIGR01846. type_I_sec_HlyB. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
PS50990. PEPTIDASE_C39. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHLYBP_ECOLX
AccessioniPrimary (citable) accession number: P08716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Caution

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

Keywords - Technical termi

3D-structure, Plasmid

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.