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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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