HLYB_ECO57
ID HLYB_ECO57 Reviewed; 706 AA.
AC Q46717; Q47462; Q79D74; Q7BSV0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB;
DE AltName: Full=EHEC-HlyB protein;
GN Name=hlyB; OrderedLocusNames=L7049, ECO57PM18;
OS Escherichia coli O157:H7.
OG Plasmid pO157.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=8936317; DOI=10.1099/00221287-142-4-907;
RA Schmidt H., Kernbach C., Karch H.;
RT "Analysis of the EHEC hly operon and its location in the physical map of
RT the large plasmid of enterohemorrhagic Esherichia coli 0157:H7.";
RL Microbiology 142:907-914(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=9722640; DOI=10.1093/nar/26.18.4196;
RA Burland V., Shao Y., Perna N.T., Plunkett G. III, Sofia H.J.,
RA Blattner F.R.;
RT "The complete DNA sequence and analysis of the large virulence plasmid of
RT Escherichia coli O157:H7.";
RL Nucleic Acids Res. 26:4196-4204(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=9628576; DOI=10.1093/dnares/5.1.1;
RA Makino K., Ishii K., Yasunaga T., Hattori M., Yokoyama K., Yatsudo H.C.,
RA Kubota Y., Yamaichi Y., Iida T., Yamamoto K., Honda T., Han C.G.,
RA Ohtsubo A., Kasamatsu M., Hayashi T., Kuhara S., Shinagawa H.;
RT "Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an
RT enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak.";
RL DNA Res. 5:1-9(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-331.
RC STRAIN=O157:H7 / EHEC;
RA Hall R.H., Xu J., Walderhaug M.O.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ABC transporter complex HlyBD involved in
CC hemolysin export. Transmembrane domains (TMD) form a pore in the inner
CC membrane and the ATP-binding domain (NBD) is responsible for energy
CC generation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: In HlyB the peptidase C39 domain, the ATP-binding domain (NBD)
CC and the transmembrane domain (TMD) are fused.
CC -!- MISCELLANEOUS: The complex HlyBD-TolC (OMF) forms a single transport
CC channel across the two membranes, allowing direct export of alpha-
CC hemolysin. These channel is involved in type 1 secretion system (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC -!- CAUTION: Asn-9 is present instead of the conserved Cys which is
CC expected to be the active site residue of peptidase C39. Thus they are
CC presumed to be without peptidase activity. {ECO:0000305}.
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DR EMBL; X86087; CAA60043.1; -; Genomic_DNA.
DR EMBL; AF074613; AAC70117.1; -; Genomic_DNA.
DR EMBL; AB011549; BAA31775.1; -; Genomic_DNA.
DR EMBL; U12572; AAA20545.2; -; Genomic_DNA.
DR PIR; T00228; T00228.
DR RefSeq; NP_052625.1; NC_002128.1.
DR RefSeq; WP_000987091.1; NZ_SWKA01000002.1.
DR AlphaFoldDB; Q46717; -.
DR SMR; Q46717; -.
DR STRING; 155864.EDL933_p0047; -.
DR EnsemblBacteria; AAC70117; AAC70117; Z_L7049.
DR EnsemblBacteria; BAA31775; BAA31775; BAA31775.
DR GeneID; 1789727; -.
DR KEGG; ece:Z_L7049; -.
DR KEGG; ecs:pO157p19; -.
DR PATRIC; fig|386585.9.peg.22; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_95_4_6; -.
DR OMA; ERQRMTI; -.
DR Proteomes; UP000000558; Plasmid pO157.
DR Proteomes; UP000002519; Plasmid pO157.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02417; Peptidase_C39_likeA; 1.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR010132; ATPase_T1SS_HlyB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039395; Peptidase_C39-like_A.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Plasmid; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Alpha-hemolysin translocation ATP-binding protein
FT HlyB"
FT /id="PRO_0000092375"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1..125
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 154..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 468..703
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 259
FT /note="E -> D (in Ref. 1; CAA60043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 79815 MW; 9A3C6EB2C2A981EB CRC64;
MMSKCSSHNS LYALILLAQY HNITVNAETI RHQYNTHTQD FGVTEWLLAA KSIGLKAKYV
EKHFSRLSII SLPALIWRDD GKHYILSRIT KDSSRYLVYD PEQHQSLTFS RDEFEKLYQG
KVILVTSRAT VVGELAKFDF SWFIPSVVKY RRILLEVLTV SAFIQFLALI TPLFFQVVMD
KVLVHRGFST LNIITIAFII VILFEVILTG ARTYIFSHTT SRIDVELGAK LFRHLLALPV
SYFENRRVGE TVARVRELEQ IRNFLTGQAL TSVLDLFFSV IFFCVMWYYS PQLTLVILLS
LPCYVIWSLF ISPLLRRRLD DKFLRNAENQ AFLVETVTAI NTIKSMAVSP QMIATWDKQL
AGYVASSFRV NLVAMTGQQG IQLIQKSVMV ISLWMGAHLV ISGEISIGQL IAFNMLAGQV
IAPVIRLAHL WQDFQQVGIS VERLGDVLNT PVEKKSGRNI LPEIQGDIEF KNVRFRYSSD
GNVILNNINL YISKGDVIGI VGRSGSGKST LTKLLQRFYI PETGQILIDG HDLSLADPEW
LRRQIGVVLQ ENILLNRSII DNITLASPAV SMEQAIEAAR LAGAHDFIRE LKEGYNTIVG
EQGVGLSGGQ RQRIAIARAL VTNPRILIFD EATSALDYES ENIIMKNMSR ICKNRTVIII
AHRLSTVKNA NRIIVMDNGF ISEDGTHKEL ISKKDSLYAY LYQLQA
