ID   GPSB_STRT1              Reviewed;         110 AA.
AC   Q5M1K5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=str0233;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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; CP000024; AAV61847.1; -; Genomic_DNA.
DR   RefSeq; WP_011225420.1; NC_006449.1.
DR   AlphaFoldDB; Q5M1K5; -.
DR   SMR; Q5M1K5; -.
DR   GeneID; 66898164; -.
DR   KEGG; stc:str0233; -.
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..110
FT                   /note="Cell cycle protein GpsB"
FT                   /id="PRO_0000337971"
FT   REGION          59..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          37..63
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
SQ   SEQUENCE   110 AA;  12374 MW;  BDEAAA7A8003E02F CRC64;
     MAKINLTPKK IYEQEFKTSI RGYDKTEVDE FLDDVIKDYT VYIALVKELQ EENAKLKAKA
     TSAPASRPAY ASATSEPSHA TTNIASASNY DILKRISRLE KEVFGKQIVE