OPPF_STRMU
ID OPPF_STRMU Reviewed; 308 AA.
AC P72479;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Oligopeptide transport ATP-binding protein OppF;
GN Name=oppF; OrderedLocusNames=SMU_259;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RC STRAIN=GS-5;
RA Peruzzi F., Piggot P.J., Daneo-Moore L.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014133; AAN58028.1; -; Genomic_DNA.
DR EMBL; U75477; AAB41195.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_720722.1; NC_004350.2.
DR RefSeq; WP_002262736.1; NC_004350.2.
DR AlphaFoldDB; P72479; -.
DR SMR; P72479; -.
DR STRING; 210007.SMU_259; -.
DR PRIDE; P72479; -.
DR EnsemblBacteria; AAN58028; AAN58028; SMU_259.
DR KEGG; smu:SMU_259; -.
DR PATRIC; fig|210007.7.peg.225; -.
DR eggNOG; COG4608; Bacteria.
DR HOGENOM; CLU_000604_1_23_9; -.
DR OMA; VFYKGQD; -.
DR PhylomeDB; P72479; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
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 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..308
FT /note="Oligopeptide transport ATP-binding protein OppF"
FT /id="PRO_0000092664"
FT DOMAIN 9..254
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 9
FT /note="V -> I (in Ref. 2; AAB41195)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="N -> D (in Ref. 2; AAB41195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34842 MW; E9C9D4E74435541D CRC64;
MTENRKKLVE VKNVSLTFNK GKANQVKAID NVSFNIYEGE VFGLVGESGS GKTTIGRAIL
KLYNIDKGEI DFEGETISKL KGKSLFNFRK KAQMIFQDPQ ASLNSRMKVR DIIAEGLDVH
KLVKNKADRD AKVQDLLDLV GLNKDHLTRY PHEFSGGQRQ RIGIARALAV EPKFIIADEP
ISALDVSIQA QVVNLMQKLQ HEQGLTYLFI AHDLSMVKYI SDRIGVMHWG KIVEIGTSDE
VYHHPIHPYT QSLLSAVPEP DPVLERQRIH KVYDPVDELD GQEREMREIT PGHFVLATEE
EAKAYKKK