ID   SPAT_BACIU              Reviewed;         614 AA.
AC   P33116;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Subtilin transport ATP-binding protein SpaT;
GN   Name=spaT; Synonyms=spaB, spaY;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=1539969; DOI=10.1128/aem.58.1.132-142.1992;
RA   Klein C., Kaletta C., Schnell N., Entian K.-D.;
RT   "Analysis of genes involved in biosynthesis of the lantibiotic subtilin.";
RL   Appl. Environ. Microbiol. 58:132-142(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=1735728; DOI=10.1128/jb.174.4.1417-1422.1992;
RA   Chung Y.J., Steen M.T., Hansen J.N.;
RT   "The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon
RT   that contains a homolog of the hemolysin B transport protein.";
RL   J. Bacteriol. 174:1417-1422(1992).
CC   -!- FUNCTION: Probably implicated in the export process of the lantibiotic
CC       subtilin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22770.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA22776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M86869; AAA22838.1; -; Genomic_DNA.
DR   EMBL; M83944; AAA22770.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M99263; AAA22776.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U09819; AAB91587.1; -; Genomic_DNA.
DR   PIR; B43935; B43935.
DR   AlphaFoldDB; P33116; -.
DR   SMR; P33116; -.
DR   TCDB; 3.A.1.111.2; the atp-binding cassette (abc) superfamily.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriocin transport; Cell membrane; Membrane;
KW   Nucleotide-binding; Protein transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..614
FT                   /note="Subtilin transport ATP-binding protein SpaT"
FT                   /id="PRO_0000092974"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          34..320
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          353..593
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         387..394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        39
FT                   /note="R -> A (in Ref. 2; AAA22770/AAA22776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="E -> D (in Ref. 2; AAA22770/AAA22776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        394
FT                   /note="K -> S (in Ref. 2; AAA22770/AAA22776)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407..408
FT                   /note="HE -> QQ (in Ref. 2; AAA22770/AAA22776)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   614 AA;  71188 MW;  8A2DE2EA0D36C33F CRC64;
     MEVKEQLKLK ELLFIMKQMP KTFKLIFTLE RSLFLKLIRF SIITGILPIV SLYISQELIN
     SLVTIRKEVS IVITIFLTYL GVSFFSELIS QISEFYNGKF QLNIGYKLNY KVMKKSSNLA
     LKDFENPEIY DKLERVTKEI SYKPYQIIQA IITMTTSFVT LLSSIAFLMS WNPKVSLLLL
     VIPVISLFYF LKIGQEEFFI HWKRAGKERK SWYISYILTH DFSFKELKLY NLKDYLLNKY
     WDIKKSFIEQ DTKILRKKTL LNLIYEIAVQ LVGAVIIFIA IMSAFAGKIM VGNVMSYIRS
     VSLVQNHSQS IMTSIYSIYN SNLYMNQLYE FLELKEEKSQ GHKKPIVEPI HSVVFQNVSF
     IYPNQGEQTL KHINVSLHKG ERVAIVGPNG SGKKTFIKLL TGLYEVHEGD ILINGINIKE
     LDMDSYMNQI AALFQDFMKY EMTLKENIGF GQIDKLHQTN KMHEVLDIVR ADFLKSHSSY
     QFDTQLGLWF DEGRQLSGGQ WQKIALARAY FREASLYILD EPSSALDPIA EKETFDTFFS
     LSKDKIGIFI SHRLVAAKLA DRIIVMDKGE IVGIGTHEEL LKTCPLYKKM DESENYMNPL
     EEEGSKWKEA LYQG