GPSB_STRPC
ID GPSB_STRPC Reviewed; 108 AA.
AC Q1JKN4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 70.
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};
GN OrderedLocusNames=MGAS9429_Spy1348;
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000259; ABF32535.1; -; Genomic_DNA.
DR RefSeq; WP_002983626.1; NC_008021.1.
DR AlphaFoldDB; Q1JKN4; -.
DR SMR; Q1JKN4; -.
DR EnsemblBacteria; ABF32535; ABF32535; MGAS9429_Spy1348.
DR GeneID; 57853046; -.
DR KEGG; spk:MGAS9429_Spy1348; -.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR Proteomes; UP000002433; 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..108
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337958"
FT COILED 32..69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
SQ SEQUENCE 108 AA; 12445 MW; FFD6AB77DC5796D2 CRC64;
MTSIIYSPKD IFEQEFKTSM RGFDKKEVDE FLDNVIKDYE NFNAQIEALK AENEALKKAK
FQARNTVSAT VQQPVPQPTR VAQSATNFDI LKRISKLEKE VFGKQIIE