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Database: UniProt
Entry: Q07UK0_RHOP5
LinkDB: Q07UK0_RHOP5
Original site: Q07UK0_RHOP5 
ID   Q07UK0_RHOP5            Unreviewed;       540 AA.
AC   Q07UK0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=ABC transporter related {ECO:0000313|EMBL:ABJ04384.1};
GN   OrderedLocusNames=RPE_0425 {ECO:0000313|EMBL:ABJ04384.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ04384.1};
RN   [1] {ECO:0000313|EMBL:ABJ04384.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ04384.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|ARBA:ARBA00005417}.
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DR   EMBL; CP000463; ABJ04384.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07UK0; -.
DR   STRING; 316055.RPE_0425; -.
DR   KEGG; rpe:RPE_0425; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_5; -.
DR   OrthoDB; 8133084at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42855:SF2; ABC TRANSPORTER ATP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42855; ABC TRANSPORTER ATP-BINDING SUBUNIT; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          2..258
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          325..539
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   540 AA;  59691 MW;  A2FE51A842700297 CRC64;
     MIRLDNISKQ NGHQILFIEA SAALLKGEKI GLVGPNGAGK TTLFRMITGR ELPDEGQVST
     DRGITIGYFS QDVGEMAGRS AVAEVMDGAG PVSEVAAELK ELEHALADPD RADEMEAILE
     RYGEVQHRFE ELDGYALEGR AREVLDGLSF SQEMMDGDVG KLSGGWKMRV ALARILLMRP
     DVMLLDEPSN HLDLESLIWL EQFLKGFEGA LLMTSHDREF MNRIVNKIIE IDGGTLTSYS
     GDFEFYAQQR ALADKQQQAQ FERQQAMLSK EIAFIERFKA RASHAAQVQS RVKKLDKIEK
     VDPPRRRETI AFDFLPAPRS GEDVVTLAGV HKRYGSRAIY DGLDFQVRRR ERWAVMGVNG
     AGKSTLLKLI AGATTPDQGT VAVGGSVKMG YFAQHAMDLI DGELTVFESL SEWFPQAGQG
     SLRALAGCFG FSGDDVEKKC RVLSGGEKAR LVMAKMLFDP PNFLVLDEPT NHLDMATKEM
     LITALSQFEG AMLFVSHDRH FLAELSNRVL ELTPEGIHKY GGGYTEYVAR TGHEAPGLHS
//
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