ID Q218D0_RHOPB Unreviewed; 593 AA.
AC Q218D0;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=ABC transporter related {ECO:0000313|EMBL:ABD87256.1};
GN OrderedLocusNames=RPC_1697 {ECO:0000313|EMBL:ABD87256.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD87256.1};
RN [1] {ECO:0000313|EMBL:ABD87256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD87256.1};
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., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000301; ABD87256.1; -; Genomic_DNA.
DR AlphaFoldDB; Q218D0; -.
DR STRING; 316056.RPC_1697; -.
DR KEGG; rpc:RPC_1697; -.
DR eggNOG; COG0411; Bacteria.
DR eggNOG; COG4177; Bacteria.
DR HOGENOM; CLU_006313_3_0_5; -.
DR OrthoDB; 9805029at2; -.
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; 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; 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 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 46..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 354..592
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 593 AA; 62258 MW; 702A9D1333BEF956 CRC64;
MSAGSDNMPL AVAALRGKPL LLRHLPYFLG AAIVVALAAT VSFDGYILNI LMQATTFAIA
VFGLSVVLGL CGQINLAQAA FFGFGAYAVG IGTTDFQLSY WLCLAAGCGI ALLAGAVLGA
STLRLGGHYL AMVTISFQQI VTLVMINAIW LTHGPDGVGR IGRPALFQSS QAYLAFCVAM
LALVGYFVWH LPDTRLGRAM RAVRDNELAA GVAGIDVFRT KVYAFALSAV LGGLAGGLFA
GGFSYISPDQ FSFAESIVFL TMSLLGGGAS PIGSAIGTAL LILIPEWLRF LKSVPGLYLA
IYGLSVILII RFMPDGIWGF VNAATQRWRA KAKLHAAGPP LQLSPAHVGG DIVLQVTGLA
KYFGGLKAVD NVDIAVKRGG VHALIGPNGS GKTTTLNVLS GLYRATAGEV LLDGTDVTTM
PPHLRAAAGL GRTFQNIRLF RSMTALENVV IGAERPGNTL IGNGGDAALH QRAMSALAFV
GLGARANELI SSFSYGHQRL IEIARALAAN PTLLLLDEPA AGLNSSEKLE LHELLKRIAA
QGLTILIIDH DMTLVSEAAQ HITVLNFGRR IADGESMAVL RHPDVVSAYL GSE
//
