ID GPSB_LISMO Reviewed; 113 AA.
AC Q8Y614;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 22-FEB-2023, entry version 96.
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=lmo1888;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000303|PubMed:29215169};
RX PubMed=29215169; DOI=10.1111/mmi.13893;
RA Rismondo J., Wamp S., Aldridge C., Vollmer W., Halbedel S.;
RT "Stimulation of PgdA-dependent peptidoglycan N-deacetylation by GpsB-PBP A1
RT in Listeria monocytogenes.";
RL Mol. Microbiol. 107:472-487(2018).
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene have increased lysozyme
CC resistance, which is important for escape from the host innate immune
CC response. The lysozyme resistance is OatA-independent, but is dependent
CC on PgdA, and an increased N-deacetylation of the peptidoglycan is
CC observed in these cells. The phenotype is suppressed by the concomitant
CC deletion of gpsB and pbpA1. {ECO:0000269|PubMed:29215169}.
CC -!- SIMILARITY: Belongs to the GpsB family. {ECO:0000255|HAMAP-
CC Rule:MF_02011}.
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DR EMBL; AL591981; CAC99966.1; -; Genomic_DNA.
DR PIR; AH1310; AH1310.
DR RefSeq; NP_465412.1; NC_003210.1.
DR RefSeq; WP_003722998.1; NZ_CP023861.1.
DR PDB; 4UG1; X-ray; 1.60 A; A/B=1-73.
DR PDBsum; 4UG1; -.
DR AlphaFoldDB; Q8Y614; -.
DR SMR; Q8Y614; -.
DR STRING; 169963.lmo1888; -.
DR PaxDb; Q8Y614; -.
DR EnsemblBacteria; CAC99966; CAC99966; CAC99966.
DR GeneID; 985801; -.
DR KEGG; lmo:lmo1888; -.
DR PATRIC; fig|169963.11.peg.1934; -.
DR eggNOG; COG3599; Bacteria.
DR HOGENOM; CLU_140309_1_0_9; -.
DR OMA; MEQVKYT; -.
DR OrthoDB; 389699at2; -.
DR PhylomeDB; Q8Y614; -.
DR BioCyc; LMON169963:LMO1888-MON; -.
DR PHI-base; PHI:5373; -.
DR Proteomes; UP000000817; 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 Gene3D; 6.10.250.660; -; 1.
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:SF1; CELL CYCLE PROTEIN GPSB; 1.
DR PANTHER; PTHR35794; CELL DIVISION PROTEIN DIVIVA; 1.
DR Pfam; PF05103; DivIVA; 1.
DR PIRSF; PIRSF029938; UCP029938; 1.
DR TIGRFAMs; TIGR03544; DivI1A_domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell shape; Coiled coil;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..113
FT /note="Cell cycle protein GpsB"
FT /id="PRO_0000337926"
FT COILED 36..68
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02011"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:4UG1"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4UG1"
FT HELIX 29..64
FT /evidence="ECO:0007829|PDB:4UG1"
SQ SEQUENCE 113 AA; 12883 MW; 03D708877CC0C3C4 CRC64;
MTSEQFEYHL TGKEILEKEF KTGLRGYSPE DVDEFLDMVI KDYSTFTQEI EALQAENIRL
VQELDNAPLR TSTQPAPTFQ AAAQPAGTTN FDILKRLSNL EKHVFGNKLD DNE
//