ID   Q66AG1_YERPS            Unreviewed;       715 AA.
AC   Q66AG1;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Alpha-hemolysin translocation ATP-binding protein HlyB {ECO:0000256|ARBA:ARBA00015531};
GN   OrderedLocusNames=YPTB2169 {ECO:0000313|EMBL:CAH21407.1};
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH21407.1, ECO:0000313|Proteomes:UP000001011};
RN   [1] {ECO:0000313|EMBL:CAH21407.1, ECO:0000313|Proteomes:UP000001011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC       exporter (TC 3.A.1.109) family. {ECO:0000256|ARBA:ARBA00006025}.
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DR   EMBL; BX936398; CAH21407.1; -; Genomic_DNA.
DR   RefSeq; WP_011192460.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66AG1; -.
DR   GeneID; 66841398; -.
DR   KEGG; ypo:BZ17_294; -.
DR   KEGG; yps:YPTB2169; -.
DR   PATRIC; fig|273123.14.peg.311; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd18588; ABC_6TM_CyaB_HlyB_like; 1.
DR   CDD; cd02259; Peptidase_C39_like; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR01846; type_I_sec_HlyB; 1.
DR   PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        151..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..127
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          151..430
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          463..698
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   715 AA;  80213 MW;  690BF6D7E74C44F0 CRC64;
     MENHVHSALI CASRLIRLAG LNPMDIETFS QKVAIDTSVK TTLASLQRYI VQFSQTASVR
     FKIRKQALEK IRQEQLPLAF RDRQGNFILL ARMNEQQVLL QYADDKKPQM LSYQSLADMW
     GGMILCCSHS RFDIRWFIPP LRRHRKPLMQ VLLLSLLLQF LALISPLFFQ VIMDKVLVHH
     ALTTLEVLIF ILVIVGVYEV ILKGLREYIF THTTTRVDIL LGGKLFQHLI RLPLSYFKQR
     HVGNIVARVR ELDNIRDFIT GSALTLCVDV VFTFVLFIVM WCISPLLTLI ILSTLPFYLL
     LAVMTTRPLQ KKVEALCGFA AQNGAFLTET VSGVETVKSL ALEPRMRQRW ESQTRDFAQA
     NFQVQNLQNL SSQAAQLLQK VAGALVIVIG AYHVMFVQLS IGQLIAFNML ALQALMPMSK
     LVDLWQQSIR AQVGLKLISD ILSLPVEPEA DPAAPHPAIS GNILLKNVAF RYRPDLDPVL
     HDLNLSIRAG EHIGLVGPSG SGKSTVARLL QRLYNTEQGV ITIDGYPINH LSPEYLRRQV
     GVVMQESYLF NRTVRENIAH SRPTATLTEV VNAASLAGAN AFILALPLGY DTVLSEGGSS
     LSGGQRQRIA IARTLLANPR ILIFDEATSA LDDESQSEIQ KNMARIIANR TVITIAHRLS
     TVRHCHRIAV ITQGRVTELA SHDELLQLNG SYARLWQQQV HFNQNKSTLT KTSPP
//