ID   GPSB_STRS2              Reviewed;         111 AA.
AC   A4VZM2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=SSU98_0403;
OS   Streptococcus suis (strain 98HAH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98HAH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA   Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA   Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA   Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT   of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(2007).
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; CP000408; ABP91561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4VZM2; -.
DR   SMR; A4VZM2; -.
DR   KEGG; ssv:SSU98_0403; -.
DR   HOGENOM; CLU_140309_1_0_9; -.
DR   OMA; MEQVKYT; -.
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..111
FT                   /note="Cell cycle protein GpsB"
FT                   /id="PRO_0000337968"
FT   REGION          59..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          32..63
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
FT   COMPBIAS        60..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   111 AA;  12867 MW;  C1EBDA8E933900D9 CRC64;
     MASIKFTTKD IFEQDFKIGF RGYDQDEVND FLDDIMKDYD AYEAIIKELK GEIARLKAQA
     ANSPKTTLPT EESNDVLRTE RPSSATNFDI LRRLNRLEKE VFGKQIVQDQ E