Y3323_BACC1
ID Y3323_BACC1 Reviewed; 553 AA.
AC Q734T1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative ABC transporter ATP-binding protein BCE_3323;
DE EC=7.-.-.-;
GN OrderedLocusNames=BCE_3323;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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}.
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DR EMBL; AE017194; AAS42231.1; -; Genomic_DNA.
DR RefSeq; WP_000367697.1; NC_003909.8.
DR AlphaFoldDB; Q734T1; -.
DR SMR; Q734T1; -.
DR EnsemblBacteria; AAS42231; AAS42231; BCE_3323.
DR GeneID; 59159269; -.
DR KEGG; bca:BCE_3323; -.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; YEACPND; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Repeat;
KW Translocase; Transport.
FT CHAIN 1..553
FT /note="Putative ABC transporter ATP-binding protein
FT BCE_3323"
FT /id="PRO_0000091975"
FT DOMAIN 7..245
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 295..527
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 553 AA; 62852 MW; 83E2DEC59BE1C27B CRC64;
MDMVAHAEIN NLSFVYADEN EKALQHISLS VQKGEFIALA GGSGSGKTTL LKHLKKELLP
IGKRTGDTYY DGTLLENVPD LLSAQEIGMV FQNPENQLVM DTVIQELAFS LENIGLPSHI
IQKRIAELIS FLGFQDLLHQ SVHTLSGGQK QLVNLAAVLV MQPKLLLLDE PTAQLDPIAA
KEFLGLLKRI NEELGITIVL SEHRLDEVIP LATRVICMNN GRIVYDGSPK RVIANMWEVE
GFRPFIPQIP RLFLEWNAKD IPFTVREAQM KMNDFSAISY VNEPIVQREK QEVILSAEHI
SFQYEKNSPL ILRDLTVSIE KGKWVALVGK NGTGKSTLLT ILAGLQKARR GKVKWNGKVI
HKIDSKERFK SIGYVSQHPY YHFTFDTVWD EVYERARELY GEQGKEIAEQ QLKKFWLYAL
KERHPHDCSG GEQQLLALCT TLLSKPTLLL LDEPTKGLDP WKKERVGELF RKLQKEGTTI
VMATHDIEFA AKYVDQCMML FDGAVIMNDA PKEFFSGNFF YTTSINRFIR KELPYALTWE
DVYEACPNDM LHS