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Protein

Alpha-hemolysin translocation ATP-binding protein HlyB

Gene

hlyB

Organism
Escherichia coli
Status
Reviewed-Annotation score: -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.

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

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

  • protein secretion by the type I secretion system Source: InterPro
  • secretion by cell Source: CAFA
  • toxin transport Source: CAFA

Keywordsi

Molecular functionHydrolase
Biological processTransport
LigandATP-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 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_00000923711 – 707Alpha-hemolysin translocation ATP-binding protein HlyBAdd BLAST707

Proteomic databases

PRIDEiP08716

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-28120N

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi467 – 478Combined sources12
Beta strandi483 – 493Combined sources11
Beta strandi497 – 501Combined sources5
Helixi508 – 515Combined sources8
Beta strandi522 – 528Combined sources7
Turni533 – 535Combined sources3
Helixi538 – 544Combined sources7
Beta strandi545 – 548Combined sources4
Beta strandi556 – 558Combined sources3
Helixi559 – 563Combined sources5
Turni564 – 566Combined sources3
Helixi572 – 581Combined sources10
Helixi585 – 589Combined sources5
Beta strandi591 – 593Combined sources3
Helixi594 – 596Combined sources3
Beta strandi598 – 600Combined sources3
Turni601 – 603Combined sources3
Helixi608 – 620Combined sources13
Beta strandi625 – 629Combined sources5
Turni632 – 635Combined sources4
Helixi638 – 652Combined sources15
Beta strandi655 – 660Combined sources6
Helixi664 – 667Combined sources4
Beta strandi670 – 677Combined sources8
Beta strandi680 – 685Combined sources6
Helixi687 – 691Combined sources5
Helixi697 – 705Combined sources9

3D structure databases

ProteinModelPortaliP08716
SMRiP08716
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08716

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

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
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.

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

Similar proteinsi

Entry informationi

Entry nameiHLYBP_ECOLX
AccessioniPrimary (citable) accession number: P08716
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: December 20, 2017
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

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

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