ID   GPSB_STAAB              Reviewed;         114 AA.
AC   Q2YY60;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=SAB1310c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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; AJ938182; CAI80999.1; -; Genomic_DNA.
DR   RefSeq; WP_001286320.1; NC_007622.1.
DR   AlphaFoldDB; Q2YY60; -.
DR   SMR; Q2YY60; -.
DR   KEGG; sab:SAB1310c; -.
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..114
FT                   /note="Cell cycle protein GpsB"
FT                   /id="PRO_0000337931"
FT   REGION          74..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          42..77
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
FT   COMPBIAS        76..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   114 AA;  13151 MW;  1A3CB7A5E8E0BA4B CRC64;
     MSDVSLKLSA KDIYEKDFEK TMARGYRREE VDAFLDDIIA DYQKMADMNN EVVKLSEENH
     KLKKELEELR LRVATSRPQD NKSFSSNNTT TNTSSNNVDI LKRISNLEKA VFGK