ID   GPSB_LACCB              Reviewed;         131 AA.
AC   B3WEI0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=LCABL_17000;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; FM177140; CAQ66781.1; -; Genomic_DNA.
DR   RefSeq; WP_003565600.1; NC_010999.1.
DR   AlphaFoldDB; B3WEI0; -.
DR   SMR; B3WEI0; -.
DR   KEGG; lcb:LCABL_17000; -.
DR   HOGENOM; CLU_140309_1_0_9; -.
DR   OMA; MEQVKYT; -.
DR   OrthoDB; 1673442at2; -.
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..131
FT                   /note="Cell cycle protein GpsB"
FT                   /id="PRO_1000189495"
FT   REGION          111..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..76
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
FT   COMPBIAS        115..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   131 AA;  15051 MW;  8FEBEBB6FA307204 CRC64;
     MDSNKETKFS IQYGPKDILD KKFKNKVRGY DPDEVDEFLD GIIRDYEAFT NEIDRLKEEN
     TKLFSRVDEL TKQLSVSKNV SAQTPQTNAA ATNYDILKRL SNLERHVFGS KLSDSSVDNH
     DDGNHSDVDQ Y