ID A0A163YET6_9BRAD Unreviewed; 599 AA.
AC A0A163YET6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=A4A58_08360 {ECO:0000313|EMBL:KZD22079.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD22079.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD22079.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD22079.1,
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KZD22079.1}.
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DR EMBL; LVYV01000023; KZD22079.1; -; Genomic_DNA.
DR RefSeq; WP_068734439.1; NZ_LVYV01000023.1.
DR AlphaFoldDB; A0A163YET6; -.
DR STRING; 943830.A4A58_08360; -.
DR OrthoDB; 9805029at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IEA:InterPro.
DR CDD; cd03219; ABC_Mj1267_LivG_branched; 1.
DR CDD; cd06581; TM_PBP1_LivM_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001851; ABC_transp_permease.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR032823; BCA_ABC_TP_C.
DR InterPro; IPR043428; LivM-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45772:SF5; BRANCHED-CHAIN AMINO ACID TRANSPORT ATP-BINDING PROTEIN LIVG-RELATED; 1.
DR PANTHER; PTHR45772; CONSERVED COMPONENT OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF12399; BCA_ABC_TP_C; 1.
DR Pfam; PF02653; BPD_transp_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 352..599
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 599 AA; 63177 MW; C9D405D3D0166693 CRC64;
MTAIADIPTS RETTTRHSVL PALLPFLGVF VLAMILPFVS NDYWALIGTR AAIYWVLVAG
LNLVVGFAGH LAIGYVALLT LGAYTTSVLA AGNVLPPVPI YGALIIASCV GAVFGVIVGL
PAMRLRTFYF AMTTLGFATI VTQIALAWQS VTGGGIGIVG PEFSAPFNTP WGFYYLCIGF
AAVATWLSAN IAYSRFGRAL IAIRDADVAA EATGISKPKL LVSIFLLAGA MAAFAGGLFA
SLQTYITPDA FTFDLSVLFF IAILIGGRGS ILGPMLGTII LTILPEIAAP LAAWSTFLYA
VLLLLIVLVM PGGIAALLDF KSRRPLASNR AIVPRIAGLS EVLRKTATTK TLTLREVVLT
FGNVRAIDGL DLDVKPGQIH GLIGPNGSGK TTTLNVISGY YAAKGGTITL GDDALPPGMP
ELRAGKGIAR TFQTPRVIGE ASVLENVMVG GTIEGEATFA EALLSLPRHH RDERKLTAQA
RAMLGVVGLE ALADVRADRL QHSELRFIEI ARALMLQPDF LLLDEPAAGL SSDEITRLGA
LIKAISRRGT GVLLVEHHAD LIFDICDQVT VLNLGKILAA GTPAEIRVHK EVVSAYLGG
//
