Y1368_CLOAB
ID Y1368_CLOAB Reviewed; 279 AA.
AC Q97JB8;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative ABC transporter ATP-binding protein CA_C1368;
DE EC=7.-.-.-;
GN OrderedLocusNames=CA_C1368;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79336.1; -; Genomic_DNA.
DR PIR; E97068; E97068.
DR RefSeq; NP_347996.1; NC_003030.1.
DR RefSeq; WP_010964677.1; NC_003030.1.
DR AlphaFoldDB; Q97JB8; -.
DR SMR; Q97JB8; -.
DR STRING; 272562.CA_C1368; -.
DR TCDB; 3.A.1.23.2; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAK79336; AAK79336; CA_C1368.
DR GeneID; 44997873; -.
DR KEGG; cac:CA_C1368; -.
DR PATRIC; fig|272562.8.peg.1573; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; DIVPLYC; -.
DR OrthoDB; 1752365at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR005876; Co_trans_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01166; cbiO; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..279
FT /note="Putative ABC transporter ATP-binding protein
FT CA_C1368"
FT /id="PRO_0000091997"
FT DOMAIN 4..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 279 AA; 31029 MW; 96C757DC305AD077 CRC64;
MNQISINNVD YIYSDGFEAL HDINMSIKKG ERVAILGPNG AGKSTLFNML NGIISPTSGE
VKINGLDTKV KKNLNVIRRD VGMVFQDSDD QLFNSSVMQE IAYGLVNMKV SEEELQSRVK
WALNVVNMDG FEKKSPHNLS GGQKKRIALA SVLAMKPEVL VLDEPTVSLD PRGTIKLVKL
LKKINEEMKI TIVFSTHDMD IVPLFADKVY VLNEGKLILQ GGVKEVFNNK KVLRNINLRL
PRVAHLAEIL KSDGCIEFDE LPLTIGEIRK CIKNLKGGI