ID   GPSB_LIMRD              Reviewed;         120 AA.
AC   A5VK11;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Lreu_0923;
OS   Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20016;
RX   PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA   Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA   Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA   Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA   Kyrpides N.C., Walter J.;
RT   "The evolution of host specialization in the vertebrate gut symbiont
RT   Lactobacillus reuteri.";
RL   PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ83185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5VK11; -.
DR   SMR; A5VK11; -.
DR   STRING; 557436.Lreu_0923; -.
DR   PRIDE; A5VK11; -.
DR   EnsemblBacteria; ABQ83185; ABQ83185; Lreu_0923.
DR   KEGG; lre:Lreu_0923; -.
DR   eggNOG; COG3599; Bacteria.
DR   HOGENOM; CLU_140309_1_0_9; -.
DR   Proteomes; UP000001991; 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_0000337922"
FT   REGION          69..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          34..74
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
SQ   SEQUENCE   120 AA;  13862 MW;  87808CFCF0627942 CRC64;
     MDNIKFTPQD ILHKQFKERN IGKGYDEADV DAFLDDVIKD YDTYNKELER LNDENERLRA
     KVDELNRQVE VGSSMSNQTA SRQPVSSATN MDILKRLSNL ERRVFGSQLD GNDNNDSHLL