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GPSB_BACSU
ID   GPSB_BACSU              Reviewed;          98 AA.
AC   P0CI74; A3F2S7; P50839;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cell cycle protein GpsB;
DE   AltName: Full=Guiding PBP1-shuttling protein;
GN   Name=gpsB; Synonyms=ypsB; OrderedLocusNames=BSU22180;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-98.
RC   STRAIN=168, 168 / PY79, 168 / SMY, 23, GSY505, MU8U5U1, NCIB3610, PS832,
RC   SB19, and SB491;
RA   Zeigler D.R.;
RT   "Reconstructing the early history of Bacillus subtilis genetics through
RT   comparative genomics.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INDUCTION BY HIGH-SALT CONDITIONS.
RC   STRAIN=168 / JH642;
RX   PubMed=14563871; DOI=10.1128/jb.185.21.6358-6370.2003;
RA   Steil L., Hoffmann T., Budde I., Volker U., Bremer E.;
RT   "Genome-wide transcriptional profiling analysis of adaptation of Bacillus
RT   subtilis to high salinity.";
RL   J. Bacteriol. 185:6358-6370(2003).
RN   [5]
RP   FUNCTION IN CELL DIVISION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH EZRA; MREC AND PBP1.
RC   STRAIN=168;
RX   PubMed=18363795; DOI=10.1111/j.1365-2958.2008.06210.x;
RA   Claessen D., Emmins R., Hamoen L.W., Daniel R.A., Errington J.,
RA   Edwards D.H.;
RT   "Control of the cell elongation-division cycle by shuttling of PBP1 protein
RT   in Bacillus subtilis.";
RL   Mol. Microbiol. 68:1029-1046(2008).
RN   [6]
RP   FUNCTION IN CELL DIVISION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   DIVISOME PROTEINS.
RC   STRAIN=168 / PY79;
RX   PubMed=18776011; DOI=10.1128/jb.00064-08;
RA   Tavares J.R., de Souza R.F., Meira G.L.S., Gueiros-Filho F.J.;
RT   "Cytological characterization of YpsB, a novel component of the Bacillus
RT   subtilis divisome.";
RL   J. Bacteriol. 190:7096-7107(2008).
CC   -!- FUNCTION: Divisome component that associates with the complex late in
CC       its assembly, after the Z-ring is formed, and is dependent on DivIC and
CC       PBP2B for its recruitment to the divisome. Together with EzrA, is a key
CC       component of the system that regulates PBP1 localization during cell
CC       cycle progression. Its main role could be the removal of PBP1 from the
CC       cell pole after pole maturation is completed. Also contributes to the
CC       recruitment of PBP1 to the division complex. Not essential for septum
CC       formation. {ECO:0000269|PubMed:18363795, ECO:0000269|PubMed:18776011}.
CC   -!- SUBUNIT: Forms polymers through the coiled coil domains. Interacts with
CC       PBP1, MreC and EzrA. {ECO:0000269|PubMed:18363795,
CC       ECO:0000269|PubMed:18776011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18363795,
CC       ECO:0000269|PubMed:18776011}. Note=Shuttles between the lateral wall
CC       and the division site in a cell cycle-dependent manner.
CC   -!- INDUCTION: By high-salt conditions. {ECO:0000269|PubMed:14563871}.
CC   -!- SIMILARITY: Belongs to the GpsB family. {ECO:0000305}.
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DR   EMBL; L47838; AAB38472.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14135.1; -; Genomic_DNA.
DR   EMBL; EF191442; ABN11504.1; -; Genomic_DNA.
DR   EMBL; EF191443; ABN11505.1; -; Genomic_DNA.
DR   EMBL; EF191444; ABN11506.1; -; Genomic_DNA.
DR   EMBL; EF191447; ABN11509.1; -; Genomic_DNA.
DR   EMBL; EF191449; ABN11510.1; -; Genomic_DNA.
DR   EMBL; EF191448; ABN11511.1; -; Genomic_DNA.
DR   EMBL; EF191450; ABN11512.1; -; Genomic_DNA.
DR   EMBL; EF191451; ABN11513.1; -; Genomic_DNA.
DR   EMBL; EF191452; ABN11514.1; -; Genomic_DNA.
DR   EMBL; EF191453; ABN11515.1; -; Genomic_DNA.
DR   EMBL; EF191454; ABN11516.1; -; Genomic_DNA.
DR   PIR; E69941; E69941.
DR   RefSeq; NP_390100.1; NC_000964.3.
DR   RefSeq; WP_003225629.1; NZ_JNCM01000036.1.
DR   PDB; 4UG3; X-ray; 2.80 A; A/B/C/D=1-68.
DR   PDB; 5AN5; X-ray; 1.20 A; B/C/D/E/F/G/H/I/J=76-98.
DR   PDB; 6GP7; X-ray; 1.95 A; A/B=5-64.
DR   PDB; 6GPZ; X-ray; 1.60 A; A/B=5-64.
DR   PDBsum; 4UG3; -.
DR   PDBsum; 5AN5; -.
DR   PDBsum; 6GP7; -.
DR   PDBsum; 6GPZ; -.
DR   AlphaFoldDB; P0CI74; -.
DR   SMR; P0CI74; -.
DR   BioGRID; 856653; 3.
DR   IntAct; P0CI74; 4.
DR   STRING; 224308.BSU22180; -.
DR   jPOST; P0CI74; -.
DR   PaxDb; P0CI74; -.
DR   PRIDE; P0CI74; -.
DR   EnsemblBacteria; CAB14135; CAB14135; BSU_22180.
DR   GeneID; 64303997; -.
DR   GeneID; 939054; -.
DR   KEGG; bsu:BSU22180; -.
DR   PATRIC; fig|224308.179.peg.2422; -.
DR   eggNOG; COG3599; Bacteria.
DR   OMA; MEQVKYT; -.
DR   PhylomeDB; P0CI74; -.
DR   BioCyc; BSUB:BSU22180-MON; -.
DR   PRO; PR:P0CI74; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02011; GpsB; 1.
DR   InterPro; IPR011229; Cell_cycle_GpsB.
DR   InterPro; IPR019933; DivIVA_domain.
DR   InterPro; IPR007793; DivIVA_fam.
DR   PANTHER; PTHR35794; PTHR35794; 1.
DR   PANTHER; PTHR35794:SF1; PTHR35794:SF1; 1.
DR   Pfam; PF05103; DivIVA; 1.
DR   PIRSF; PIRSF029938; UCP029938; 1.
DR   TIGRFAMs; TIGR03544; DivI1A_domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell shape; Coiled coil;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..98
FT                   /note="Cell cycle protein GpsB"
FT                   /id="PRO_0000049725"
FT   COILED          34..71
FT                   /evidence="ECO:0000255"
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:6GPZ"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:6GPZ"
FT   HELIX           27..62
FT                   /evidence="ECO:0007829|PDB:6GPZ"
FT   HELIX           76..92
FT                   /evidence="ECO:0007829|PDB:5AN5"
SQ   SEQUENCE   98 AA;  11592 MW;  3B54837F07A00A9C CRC64;
     MLADKVKLSA KEILEKEFKT GVRGYKQEDV DKFLDMIIKD YETFHQEIEE LQQENLQLKK
     QLEEASKKQP VQSNTTNFDI LKRLSNLEKH VFGSKLYD
 
 
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