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Database: UniProt
Entry: A0A0X8CMP9_9BRAD
LinkDB: A0A0X8CMP9_9BRAD
Original site: A0A0X8CMP9_9BRAD 
ID   A0A0X8CMP9_9BRAD        Unreviewed;       568 AA.
AC   A0A0X8CMP9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AMA60196.1};
GN   ORFNames=BCCGELA001_30885 {ECO:0000313|EMBL:AMA60196.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA60196.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA60196.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA60196.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(2014).
CC   -!- FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains
CC       (TMD) form a pore in the inner membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation.
CC       {ECO:0000256|ARBA:ARBA00024722}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004417}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|ARBA:ARBA00005417}.
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DR   EMBL; CP013949; AMA60196.1; -; Genomic_DNA.
DR   RefSeq; WP_060737028.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A0X8CMP9; -.
DR   STRING; 1223566.BCCGELA001_30885; -.
DR   KEGG; brc:BCCGELA001_30885; -.
DR   Proteomes; UP000019052; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015833; P:peptide transport; IEA:InterPro.
DR   CDD; cd03257; ABC_NikE_OppD_transporters; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43776:SF6; DIPEPTIDE TRANSPORT ATP-BINDING PROTEIN DPPF; 1.
DR   PANTHER; PTHR43776; TRANSPORT ATP-BINDING PROTEIN; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF08352; oligo_HPY; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:AMA60196.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          16..266
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          306..549
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   568 AA;  61623 MW;  8DB8D5AAF7D2CB23 CRC64;
     MLQVLNRQGL PQADLLTVDS LRVSFGRDFP EGTAVRGVSF SLQAGRCLAI VGGSGSGKSV
     TARAIVGLAG PRAHVRARQL KLAGTDLTAL DDRSWRRVRG KEIGFVLQDA LVALDPLRPV
     GKEIGEALRL HRAAASREEL ERRVVALLEL VGVPEAEVKA RQLPHQLSGG QRQRALIAAA
     LALDPGILIA DEPTTALDVT VQAQVLGLLE ETKVRGKALI LISHDLAVVS QIADEVLVMH
     EGKVVERGSA DQVFQDPQHA YTRQLLDAVP SALPRGSRPS LLPGIWPKPR SRSREELPST
     FPSVVLSAAK LVKRFKGPDG VLRTAVDGVS FELRSGETLG VVGESGSGKS TMARMALALD
     LPDEGTVSFQ GQAWTTIAER DRRARRRAIS VIYQDPLSSF DPRWSVGRII SDSLAGDLAT
     NGERDQRVVQ LLDLVGLSPT FRDRRPLELS GGQRQRVAIA RAIAPRPAVI VCDEPVSALD
     VLVQAQVLDL LTNLKAHLNM SYIFISHDLG VVRQLSDRVM VMRQGRVVET GTRDEIFLDP
     RTDYTQRLLA AVPNLERRGA GSRSFGRV
//
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