GPSB_STRA3
ID GPSB_STRA3 Reviewed; 110 AA.
AC Q8E766;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Cell cycle protein GpsB {ECO:0000255|HAMAP-Rule:MF_02011};
DE AltName: Full=Guiding PBP1-shuttling protein {ECO:0000255|HAMAP-Rule:MF_02011};
GN Name=gpsB {ECO:0000255|HAMAP-Rule:MF_02011}; OrderedLocusNames=gbs0291;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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:0000255|HAMAP-Rule:MF_02011}.
CC -!- SUBUNIT: Forms polymers through the coiled coil domains. Interacts with
CC PBP1, MreC and EzrA. {ECO:0000255|HAMAP-Rule:MF_02011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02011}.
CC Note=Shuttles between the lateral wall and the division site in a cell
CC cycle-dependent manner. {ECO:0000255|HAMAP-Rule:MF_02011}.
CC -!- SIMILARITY: Belongs to the GpsB family. {ECO:0000255|HAMAP-
CC Rule:MF_02011}.
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DR EMBL; AL766844; CAD45936.1; -; Genomic_DNA.
DR RefSeq; WP_000146544.1; NC_004368.1.
DR AlphaFoldDB; Q8E766; -.
DR SMR; Q8E766; -.
DR STRING; 211110.gbs0291; -.
DR EnsemblBacteria; CAD45936; CAD45936; CAD45936.
DR GeneID; 66885274; -.
DR KEGG; san:gbs0291; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR Proteomes; UP000000823; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell shape; Coiled coil; Cytoplasm.
FT CHAIN 1..110
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337949"
FT COILED 32..73
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
SQ SEQUENCE 110 AA; 13016 MW; 7FCC0326719154CD CRC64;
MASIIYSPKD IFEQDFKVSM RGYDKKEVDV FLDDVIKDYE NYLEQIEKLQ MENRRLQQAL
DKKESEASNV RNSGTAMYNQ KPIAQSATNF DILKRISRLE KEVFGRQIRE