Q47258 (HLYB3_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-hemolysin translocation ATP-binding protein HlyB

Gene names

Name:

hlyB

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cell inner membrane; Multi-pass membrane protein Probable.
Domain	In HlyB the peptidase C39 domain, the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
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.
Sequence similarities	Belongs to the ABC transporter superfamily. Protein-1 exporter (TC 3.A.1.109) family. [View classification] Contains 1 ABC transmembrane type-1 domain. Contains 1 ABC transporter domain. Contains 1 peptidase C39 domain.
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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	protein secretion by the type I secretion system Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell type I protein secretion system complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of substances Inferred from electronic annotation. Source: InterPro peptidase activity Inferred from electronic annotation. Source: InterPro protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 707	707	Alpha-hemolysin translocation ATP-binding protein HlyB		PRO_0000092373
Regions
	Transmembrane	158 – 178	21	Helical; Potential
	Transmembrane	191 – 211	21	Helical; Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Transmembrane	295 – 315	21	Helical; Potential
	Transmembrane	388 – 408	21	Helical; Potential
	Domain	3 – 125	123	Peptidase C39
	Domain	154 – 436	283	ABC transmembrane type-1
	Domain	468 – 703	236	ABC transporter
	Nucleotide binding	502 – 509	8	ATP Potential
Sites
	Active site	83	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q47258 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E709E59F21BDA853	FASTA	707	79,529
	10 20 30 40 50 60 MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV 70 80 90 100 110 120 KKTIDRLNFI SLPALVWRED GRHFILTKVS KEANRYLIFD LEQRNPRVLE QSEFEALYQG 130 140 150 160 170 180 HIILIASRSS VAGKLAKFDF TWFIPAIIKY RRIFIETLVV SVFLQLFALI TPLFFQVVMD 190 200 210 220 230 240 KVLVHRGFST LNVITVALSV VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI 250 260 270 280 290 300 SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS 310 320 330 340 350 360 LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL 370 380 390 400 410 420 AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI 430 440 450 460 470 480 VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTESYHGKLA LPEINGDITF RNIRFRYKPD 490 500 510 520 530 540 SPVILDNINL SIKQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW 550 560 570 580 590 600 LRRQVGVVLQ DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG 610 620 630 640 650 660 EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHIIMRNMHK ICKGRTVIII 670 680 690 700 AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD

References

[1]	"Characterization of the hemolysin transporter, HlyB, using an epitope insertion." Juranka P., Zhang F., Kulpa J., Endicott J.A., Blight M., Holland I.B., Ling V. J. Biol. Chem. 267:3764-3770(1992) [PubMed: 1371277] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LE2001 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M81823 Genomic DNA. Translation: AAA23978.1.
PIR	LEECB. A42255.
3D structure databases
ProteinModelPortal	Q47258.
SMR	Q47258. Positions 467-707.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR001140. ABC_transptr_TM_dom. IPR011527. ABC_transptrTM_dom_typ1. IPR003593. ATPase_AAA+_core. IPR010132. ATPase_T1SS_HlyB. IPR005074. Peptidase_C39. [Graphical view]
Pfam	PF00664. ABC_membrane. 1 hit. PF00005. ABC_tran. 1 hit. PF03412. Peptidase_C39. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF90123. ABC_TM_1. 1 hit.
TIGRFAMs	TIGR01846. Type_I_sec_HlyB. 1 hit.
PROSITE	PS50929. ABC_TM1F. 1 hit. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. PS50990. PEPTIDASE_C39. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HLYB3_ECOLX

Accession

Primary (citable) accession number: Q47258

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program