GPSB_STAHJ
ID GPSB_STAHJ Reviewed; 112 AA.
AC Q4L6F0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=SH1466;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04775.1; -; Genomic_DNA.
DR RefSeq; WP_011275761.1; NC_007168.1.
DR AlphaFoldDB; Q4L6F0; -.
DR SMR; Q4L6F0; -.
DR STRING; 279808.SH1466; -.
DR EnsemblBacteria; BAE04775; BAE04775; SH1466.
DR GeneID; 58062331; -.
DR KEGG; sha:SH1466; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR OrthoDB; 1673442at2; -.
DR Proteomes; UP000000543; 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..112
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337947"
FT REGION 75..97
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..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 112 AA; 12856 MW; FC9563AD3DD871E5 CRC64;
MADVSLKLSA KDIYEKDFEK TMARGYRREE VDAFLDDIIT DYQKMADMNN EVVKLSEENN
KLKKEVEELR LRVATSRPSD NKSFSSNNSS SSNNNVDILK RISNLEKAVF GK