ID   Y2655_BACCR             Reviewed;         566 AA.
AC   Q81CT8;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Putative ABC transporter ATP-binding protein BC_2655;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=BC_2655;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC       energy coupling to the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP09613.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016877; AAP09613.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_832412.1; NC_004722.1.
DR   RefSeq; WP_001182509.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81CT8; -.
DR   SMR; Q81CT8; -.
DR   STRING; 226900.BC_2655; -.
DR   EnsemblBacteria; AAP09613; AAP09613; BC_2655.
DR   KEGG; bce:BC2655; -.
DR   PATRIC; fig|226900.8.peg.2702; -.
DR   HOGENOM; CLU_000604_86_7_9; -.
DR   OMA; DPMTRLD; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR022216; ABC_Co_transporter.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12558; DUF3744; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..566
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   BC_2655"
FT                   /id="PRO_0000091979"
FT   DOMAIN          5..246
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          300..533
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   566 AA;  63929 MW;  A458933B5BCD003D CRC64;
     MQPIISFEQF TFQYGHAAQP TLSDITFHIY PGEKVLIAGR SGSGKSTLAH CINGLIPFSY
     EGNSTGNVLI AGKDPREGSI FEQSKQVGTI LQDQDAQFIG LTVEEDVAFY LENECVKQDN
     MKKIVSDSLR KVKMHTFHKQ SPHELSGGQK QTVSLAGLLT TNADILLFDE PLANLDPLSA
     IHTIELMKDI HEQYNKTIVI IEHRIEEIFK LDLDKVILID EGKVIAMGTP KEILASNILP
     RIGLREPIYI EALKRLHFDS NNDVIYPMEN LQKEKVSNVI KEWMEKQVIL KRNAKNKELL
     KVENLSFSYP NKQKVLENVN LLIYEGEIVA LLGHNGAGKS TLAHSLIGIN KMKNGKIALK
     GEDISSWSIR KRGEIISYVM QNPNHMITQP TVFEEVSFTL TLHNFSKEEI KNKVEGILKI
     CGLYPFRNWP IQALSYGQKK RLTIASVLTT NPKLIILDEP TAGQDYYHYK QFMSFIKNLA
     KKGISFVVIT HDMNLALEYT DRAVVLHEGK IIADNTVFDV LGNQETLQRA NLRESSLTKL
     IKFSGIACPE KFMELYLDST RREEGA