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Database: UniProt
Entry: J2WES1_9BRAD
LinkDB: J2WES1_9BRAD
Original site: J2WES1_9BRAD 
ID   J2WES1_9BRAD            Unreviewed;       738 AA.
AC   J2WES1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=UPF0261 protein PMI42_05519 {ECO:0000256|HAMAP-Rule:MF_00677};
GN   ORFNames=PMI42_05519 {ECO:0000313|EMBL:EJN11155.1};
OS   Bradyrhizobium sp. YR681.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN11155.1, ECO:0000313|Proteomes:UP000007272};
RN   [1] {ECO:0000313|EMBL:EJN11155.1, ECO:0000313|Proteomes:UP000007272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR681 {ECO:0000313|EMBL:EJN11155.1,
RC   ECO:0000313|Proteomes:UP000007272};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|ARBA:ARBA00005417}.
CC   -!- SIMILARITY: Belongs to the UPF0261 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00677}.
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:EJN11155.1}.
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DR   EMBL; AKIY01000238; EJN11155.1; -; Genomic_DNA.
DR   RefSeq; WP_008139382.1; NZ_AKIY01000238.1.
DR   AlphaFoldDB; J2WES1; -.
DR   PATRIC; fig|1144344.3.peg.5096; -.
DR   OrthoDB; 9776369at2; -.
DR   Proteomes; UP000007272; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03224; ABC_TM1139_LivF_branched; 1.
DR   CDD; cd15488; Tm-1-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.12030; Uncharacterised protein family UPF0261, NC domain; 1.
DR   Gene3D; 3.40.50.12020; Uncharacterised protein family UPF0261, NN domain; 1.
DR   HAMAP; MF_00677; UPF0261; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008322; UPF0261.
DR   InterPro; IPR044122; UPF0261_dom.
DR   PANTHER; PTHR31862; UPF0261 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G10120); 1.
DR   PANTHER; PTHR31862:SF1; UPF0261 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G10120); 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF06792; UPF0261; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          11..239
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          252..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  79208 MW;  8580554BA267C5C4 CRC64;
     MNEARRTAGA LEVRGLDVYY GHSHALQGVD LSLDAGVFSV VGRNGMGKTT LCKAIMGLVP
     VSGGSIRVRG EDITRRPPAH IARLGVGYVP QGRRLWRSLS VDEHLRLAGG MRSGAWTVER
     IYDTFPRLAE RKDHGGGQLS GGEQQMLAIS RALLTNPHLL IMDEPTEGLA PVIVAQVEEM
     LLQLGEDGDM SVLVIEQNIG VATAISRNVA IMVNGRINRV IDSVRLAADR ELQRRLLGVG
     LHAELEPDID VPAAGGEAKT APQPARTSGP IRIYISNPIP PTRWSQPVPI GRIEAAARTL
     STQVARLDET ARRKREPVTT QTARPPVVLV VGTLDTKGTE LRFIRDIIAE SGLRTRLIDV
     STSGKQATCD VSAQEIALNH GRGGSTVFGP DRGAAVTAMA DAFANWIRRQ GNIAGVISAG
     GSGAASLVAP GMRALPVGIP KLIISSVASG DVGPYVGPAD ITMMHSVTDV QGLNSISRAV
     LSNGANAISG MVRARLDQRE ARERAASASL PSVGITMFGV TTPAVQKIAA DLREDFECLV
     FHATGVGGRS MEKLVDSGQL AGVVDLTTTE ICDLLMGGVF PATEDRFGAV IRTRVPYVGS
     VGALDMVNFG APDTIPERYR TRKFHVHNPQ VTLMRTTVEE NERIGRWIGE RLNQMDGPVR
     FFLPEGGVSA LDASGQPFWD LEADAALFRA LERTVRQTAN RQLIRVKQNI NDPEFASTIV
     SAFRTLFGRA GARRRLAR
//
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