OPPB_BACSU
ID OPPB_BACSU Reviewed; 311 AA.
AC P24138; O31598; P24691;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Oligopeptide transport system permease protein OppB;
DE AltName: Full=Stage 0 sporulation protein KB;
GN Name=oppB; Synonyms=spo0KB; OrderedLocusNames=BSU11440;
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 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).
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:0000269|PubMed:20713508};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC Membrane raft {ECO:0000269|PubMed:20713508}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Present in detergent-resistant membrane
CC (DRM) fractions that may be equivalent to eukaryotic membrane rafts;
CC these rafts include proteins involved in signaling, molecule
CC trafficking and protein secretion. {ECO:0000269|PubMed:20713508}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62689.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X56347; CAA39788.1; -; Genomic_DNA.
DR EMBL; M57689; AAA62688.1; -; Genomic_DNA.
DR EMBL; M57689; AAA62689.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13001.1; -; Genomic_DNA.
DR PIR; H69668; H69668.
DR RefSeq; NP_389026.1; NC_000964.3.
DR RefSeq; WP_003245554.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24138; -.
DR SMR; P24138; -.
DR STRING; 224308.BSU11440; -.
DR PaxDb; P24138; -.
DR PRIDE; P24138; -.
DR EnsemblBacteria; CAB13001; CAB13001; BSU_11440.
DR GeneID; 936397; -.
DR KEGG; bsu:BSU11440; -.
DR PATRIC; fig|224308.179.peg.1230; -.
DR eggNOG; COG0601; Bacteria.
DR InParanoid; P24138; -.
DR OMA; GLQLGYM; -.
DR PhylomeDB; P24138; -.
DR BioCyc; BSUB:BSU11440-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_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..311
FT /note="Oligopeptide transport system permease protein OppB"
FT /id="PRO_0000060133"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 94..295
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 110
FT /note="A -> G (in Ref. 1; CAA39788)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..234
FT /note="RPAVTVRHAIRNALLPVVTYM -> AQRVQCGTPFETHFCRLLHIL (in
FT Ref. 2; AAA62688/AAA62689)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="V -> L (in Ref. 1; CAA39788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34075 MW; D5B61C436874A41B CRC64;
MLKYIGRRLV YMIITLFVIV TVTFFLMQAA PGGPFSGEKK LPPEIEANLN AHYGLDKPLF
VQYVSYLKSV AMWDFGPSFK YKGQSVNDLI SSGFPVSFTL GAEAILLALA LGVLFGVIAA
LYHNKWQDYT VAILTIFGIS VPSFIMAAVL QYVFSMKLGL FPVAGWDSWA YTFLPSIALA
SMPMAFIARL SRSSMIEVLN SDYIRTAKAK GLSRPAVTVR HAIRNALLPV VTYMGPMAAQ
VLTGSFIIET IFGIPGLGAH FVNSITNRDY TVIMGVTVFF SVILLLCVLI VDVLYGIIDP
RIKLSKAKKG A
