OPPA_BACSU
ID OPPA_BACSU Reviewed; 545 AA.
AC P24141; P23399;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Oligopeptide-binding protein OppA;
DE AltName: Full=Stage 0 sporulation protein KA;
DE Flags: Precursor;
GN Name=oppA; Synonyms=spo0KA; OrderedLocusNames=BSU11430;
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
RN [8]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
CC -!- FUNCTION: This protein is a component of the oligopeptide permease, a
CC binding protein-dependent transport system, It binds peptides up to
CC five amino acids long with high affinity. Also required for sporulation
CC and competence.
CC -!- SUBUNIT: Interacts with FloT in detergent-resistant membranes (DRM)
CC (PubMed:23651456). Colocalizes rarely with FloT membrane assemblies
CC (PubMed:27362352). {ECO:0000269|PubMed:23651456,
CC ECO:0000269|PubMed:27362352}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456,
CC ECO:0000305|PubMed:27362352}; Lipid-anchor {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210,
CC ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:27362352}; Lipid-anchor
CC {ECO:0000305}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; X56347; CAA39787.1; -; Genomic_DNA.
DR EMBL; M57689; AAA62687.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13000.1; -; Genomic_DNA.
DR PIR; A38447; A38447.
DR RefSeq; NP_389025.1; NC_000964.3.
DR AlphaFoldDB; P24141; -.
DR SMR; P24141; -.
DR STRING; 224308.BSU11430; -.
DR iPTMnet; P24141; -.
DR jPOST; P24141; -.
DR PaxDb; P24141; -.
DR PRIDE; P24141; -.
DR EnsemblBacteria; CAB13000; CAB13000; BSU_11430.
DR GeneID; 936398; -.
DR KEGG; bsu:BSU11430; -.
DR PATRIC; fig|224308.43.peg.1194; -.
DR eggNOG; COG4166; Bacteria.
DR InParanoid; P24141; -.
DR BioCyc; BSUB:BSU11430-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
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 InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Competence; Lipoprotein; Membrane; Palmitate;
KW Peptide transport; Phosphoprotein; Protein transport; Reference proteome;
KW Signal; Sporulation; Transport.
FT SIGNAL 1..20
FT CHAIN 21..545
FT /note="Oligopeptide-binding protein OppA"
FT /id="PRO_0000031793"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="T -> S (in Ref. 2; AAA62687/CAB13000)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> K (in Ref. 2; AAA62687/CAB13000)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="M -> I (in Ref. 2; AAA62687/CAB13000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 61525 MW; 8B4B69D9FDC4B4E6 CRC64;
MKKRWSIVTL MLIFTLVLSA CGFGGTGSNG EGKKDSKGKT TLNINIKTEP FSLHPGLAND
SVSGGVIRQT FEGLTRINAD GEPEEGMASK IETSKDGKTY TFTIRDGVKW SNGDPVTAQD
FEYAWKWALD PNNESQYAYQ LYYIKGAEAA NTGKGSLDDV AVKAVNDKTL KVELNNPTPY
FTELTAFYTY MPINEKIAEK NKKWNTNAGD DYVSNGPFKM TAWKHSGSIT LEKNDQYWDK
DKVKLKKIDM VMINNNNTEL KKFQAGELDW AGMPLGQLPT ESLPTLKKDG SLHVEPIAGV
YWYKFNTEAK PLDNVNIRKA LTYSLDRQSI VKNVTQGEQM PAMAAVPPTM KGFEDNKEGY
FKDNDVKTAK EYLEKGLKEM GLSKASDLPK IKLSYNTDDA HAKIAQAVQE MWKKNLGVDV
ELDNSEWNVY IDKLHSQDYQ IGRMGWLGDF NDPINFLELF RDKNGGNNDT GWENPEFKKL
LNQSQTETDK TKRAELLKKA EGIFIDEMPV APIYFYTDTW VQDENLKGVI MPGTGEVYFR
NAYFK
