ID A0A163X1S0_9BRAD Unreviewed; 544 AA.
AC A0A163X1S0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Microcin ABC transporter ATP-binding protein {ECO:0000313|EMBL:KZD20297.1};
GN ORFNames=A4A58_18785 {ECO:0000313|EMBL:KZD20297.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD20297.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD20297.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD20297.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC {ECO:0000256|ARBA:ARBA00005417}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZD20297.1}.
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DR EMBL; LVYV01000056; KZD20297.1; -; Genomic_DNA.
DR RefSeq; WP_068738557.1; NZ_LVYV01000056.1.
DR AlphaFoldDB; A0A163X1S0; -.
DR STRING; 943830.A4A58_18785; -.
DR OrthoDB; 9802264at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
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; PTHR43297:SF6; DIPEPTIDE TRANSPORT ATP-BINDING PROTEIN DPPD; 1.
DR PANTHER; PTHR43297; OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN APPD; 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:KZD20297.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 9..259
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 279..527
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 544 AA; 58282 MW; ABDD54D1AD70E222 CRC64;
MSAVDNPILT IDGLSVKLPK GADRSHALGG VSMAISANEI VCVVGESGSG KSVMANAIMR
LLPGEVAIDG GRVLFEGKDL ASASNAEMRK VRGAGIAMIF QEPMTALNPL RTIGDQIGEM
FEIHTELSKT EIKARVLALL QDVHIPDPAQ AARAYPHELS GGQRQRAMIA MALALDPRLL
IADEPTTALD VTTQAQILKL IKELQSRRNT AVLFITHDFG VVAEIADRVV VMQHGNVVEQ
GAVKDVLSNP QHPYTQQLIA AVPPLTAPPP RALSDDIILT LDNVSKTYRN GGFLGRGVRV
THAVKSVSLK LPRGATLGIV GESGSGKSTL ARCIIRLIDP DGGSIVLEGK DWAKLTRDEV
RRETKHIQMV FQDPFASLNP RRKAGDLVAQ GPIVHGTPRA QAVAQAKELF RLVGLDPSAI
DRFPHEFSGG QRQRIGLARA LALKPDVLVA DEAVSALDVS VQAQVLKMLH ELRERLGLSI
VFITHDLRVA AQICDLVAVM KDGEVVEHGL AGEVFGNPQH AYTKALLASI PGGDFARSRK
PVTV
//
