OPPD_MYCGE
ID OPPD_MYCGE Reviewed; 402 AA.
AC P47325;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Oligopeptide transport ATP-binding protein OppD;
GN Name=oppD; OrderedLocusNames=MG079;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC oligopeptides. Probably responsible for energy coupling to the
CC transport system (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; L43967; AAC71297.1; -; Genomic_DNA.
DR PIR; G64208; G64208.
DR RefSeq; WP_010869322.1; NC_000908.2.
DR AlphaFoldDB; P47325; -.
DR SMR; P47325; -.
DR STRING; 243273.MG_079; -.
DR EnsemblBacteria; AAC71297; AAC71297; MG_079.
DR KEGG; mge:MG_079; -.
DR eggNOG; COG0444; Bacteria.
DR HOGENOM; CLU_000604_1_23_14; -.
DR OMA; YEPAHPY; -.
DR OrthoDB; 1101128at2; -.
DR BioCyc; MGEN243273:G1GJ2-91-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
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 Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08352; oligo_HPY; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Peptide transport; Protein transport; Reference proteome; Transport.
FT CHAIN 1..402
FT /note="Oligopeptide transport ATP-binding protein OppD"
FT /id="PRO_0000092656"
FT DOMAIN 22..309
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 402 AA; 45494 MW; 60DD85496F8DF83F CRC64;
MALKRSNFFV DKDQQLKDNL ILDITDLHVN FKVKDGILHA VRGIDLKVER GSIVGIVGES
GSGKSVSVKS IIGFNDNAQT KAKLMNFKNV DITKLKKHQW KYYRGTYVSY ISQDPLFSLN
PTMTIGKQVK EAIYVASKRR YFQAKSDLKF ALSNKEIDKK TYKSKLKEIK QTYQQKIKPI
NVEKKTLEIL QFIGINDAKK RLKAFPSEFS GGMRQRIVIA IAVATEPDLI IADEPTTALD
VTIQAKVLTL IKQLRDLLNI TIIFISHNIS LIANFCDFVY VMYAGKIVEQ GLVEEIFTNP
LHPYTWALIS SIPEQKDKNK PLTSIPGVIP NMLTPPKGDA FASRNQYALA IDFEYHPPFF
EVTKTHKAAT WLLHPQAPKV EPPQAVIDNI TLTKKALQFK DQ
