GPSB_STRSV
ID GPSB_STRSV Reviewed; 120 AA.
AC A3CPY3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, 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=SSA_1857;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(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; CP000387; ABN45238.1; -; Genomic_DNA.
DR RefSeq; WP_011837411.1; NC_009009.1.
DR RefSeq; YP_001035788.1; NC_009009.1.
DR AlphaFoldDB; A3CPY3; -.
DR SMR; A3CPY3; -.
DR STRING; 388919.SSA_1857; -.
DR EnsemblBacteria; ABN45238; ABN45238; SSA_1857.
DR KEGG; ssa:SSA_1857; -.
DR PATRIC; fig|388919.9.peg.1762; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR OrthoDB; 1673442at2; -.
DR Proteomes; UP000002148; 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;
KW Reference proteome.
FT CHAIN 1..120
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337966"
FT REGION 63..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..68
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 13922 MW; A9C62E9B7F0E2B03 CRC64;
MASIIFTAKD IFDQDFKREV RGYSKSEVDE FLDDIIKDYE TYAALVKELR EENRRLKEEL
AAKPVEKAPV QPTQPVQSTQ ATQSTVESFS QMTSATNFDI LKRLNRLEKE VFGKQILDRE