GPSB_LEVBA
ID GPSB_LEVBA Reviewed; 117 AA.
AC Q03S32;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=LVIS_0848;
OS Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=387344;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC 947 / NCTC 947;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000416; ABJ63990.1; -; Genomic_DNA.
DR RefSeq; WP_011667776.1; NC_008497.1.
DR AlphaFoldDB; Q03S32; -.
DR SMR; Q03S32; -.
DR STRING; 387344.LVIS_0848; -.
DR EnsemblBacteria; ABJ63990; ABJ63990; LVIS_0848.
DR GeneID; 66420979; -.
DR KEGG; lbr:LVIS_0848; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR OrthoDB; 1673442at2; -.
DR Proteomes; UP000001652; 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..117
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337919"
FT COILED 32..70
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
SQ SEQUENCE 117 AA; 13491 MW; 696C214456916B01 CRC64;
MENVNFTPKE ILQKQFRQKM RGYDPDDVDS FLDNVIKDYD AFVKENQRLQ DENERLLAKV
DELTRQVQVG ASQPRAAATS PASSNVTNMD ILKRLSNLER HVFGSQLDND PNESHRL