OPPC_BACSU
ID OPPC_BACSU Reviewed; 305 AA.
AC P24139; P24692;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Oligopeptide transport system permease protein OppC;
DE AltName: Full=Stage 0 sporulation protein KC;
GN Name=oppC; Synonyms=spo0KC; OrderedLocusNames=BSU11450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1901616; DOI=10.1111/j.1365-2958.1991.tb01838.x;
RA Perego M., Higgins C.F., Pearce S.R., Gallagher M.P., Hoch J.A.;
RT "The oligopeptide transport system of Bacillus subtilis plays a role in the
RT initiation of sporulation.";
RL Mol. Microbiol. 5:173-185(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1899858; DOI=10.1128/jb.173.4.1388-1398.1991;
RA Rudner D.Z., Ledeaux J.R., Ireton K., Grossman A.D.;
RT "The spo0K locus of Bacillus subtilis is homologous to the oligopeptide
RT permease locus and is required for sporulation and competence.";
RL J. Bacteriol. 173:1388-1398(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC oligopeptides; probably responsible for the translocation of the
CC substrate across the membrane. Also required for sporulation and
CC competence.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; X56347; CAA39789.1; -; Genomic_DNA.
DR EMBL; M57689; AAA62690.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13002.1; -; Genomic_DNA.
DR PIR; A69669; A69669.
DR RefSeq; NP_389027.1; NC_000964.3.
DR RefSeq; WP_003232954.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24139; -.
DR SMR; P24139; -.
DR STRING; 224308.BSU11450; -.
DR PaxDb; P24139; -.
DR PRIDE; P24139; -.
DR EnsemblBacteria; CAB13002; CAB13002; BSU_11450.
DR GeneID; 936396; -.
DR KEGG; bsu:BSU11450; -.
DR PATRIC; fig|224308.179.peg.1231; -.
DR eggNOG; COG1173; Bacteria.
DR InParanoid; P24139; -.
DR OMA; TRPWLFW; -.
DR PhylomeDB; P24139; -.
DR BioCyc; BSUB:BSU11450-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR025966; OppC_N.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF12911; OppC_N; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Competence; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..305
FT /note="Oligopeptide transport system permease protein OppC"
FT /id="PRO_0000060134"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 103..292
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 36
FT /note="R -> P (in Ref. 2; AAA62690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33621 MW; 440E469DDEEEC354 CRC64;
MQNIPKNMFE PAAANAGDAE KISKKSLSLW KDAMLRFRSN KLAMVGLIII VLIILMAIFA
PMFSRYDYST TNLLNADKPP SKDHWFGTDD LGRDIFVRTW VGARISIFIG VAAAVLDLLI
GVIWGSISGF RGGRTDEIMM RIADILWAVP SLLMVILLMV VLPKGLFTII IAMTITGWIN
MARIVRGQVL QLKNQEYVLA SQTLGAKTSR LLFKHIVPNA MGSILVTMTL TVPTAIFTEA
FLSYLGLGVP APLASWGTMA SDGLPALTYY PWRLFFPAGF ICITMFGFNV VGDGLRDALD
PKLRK
