ID E8XAY5_SALT4 Unreviewed; 262 AA.
AC E8XAY5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE Flags: Precursor;
GN Name=ybgF {ECO:0000313|EMBL:ADX16492.1};
GN Synonyms=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN OrderedLocusNames=STM474_0775 {ECO:0000313|EMBL:ADX16492.1};
OS Salmonella typhimurium (strain 4/74).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX16492.1, ECO:0000313|Proteomes:UP000008978};
RN [1] {ECO:0000313|EMBL:ADX16492.1, ECO:0000313|Proteomes:UP000008978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX PubMed=21478351; DOI=10.1128/JB.00394-11;
RA Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT animals.";
RL J. Bacteriol. 193:3162-3163(2011).
CC -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and outer
CC membrane constriction during cell division. {ECO:0000256|HAMAP-
CC Rule:MF_02066}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_02066}.
CC -!- SIMILARITY: Belongs to the CpoB family. {ECO:0000256|HAMAP-
CC Rule:MF_02066}.
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DR EMBL; CP002487; ADX16492.1; -; Genomic_DNA.
DR RefSeq; WP_000097552.1; NC_016857.1.
DR AlphaFoldDB; E8XAY5; -.
DR KEGG; seb:STM474_0775; -.
DR PATRIC; fig|909946.3.peg.800; -.
DR HOGENOM; CLU_044315_4_0_6; -.
DR Proteomes; UP000008978; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR HAMAP; MF_02066; CpoB; 1.
DR InterPro; IPR034706; CpoB.
DR InterPro; IPR014162; CpoB_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR032519; YbgF_tri.
DR NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR PANTHER; PTHR37423:SF5; CELL DIVISION COORDINATOR CPOB; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF16331; TolA_bind_tri; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02066};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02066};
KW Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 27..262
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009991398"
FT DOMAIN 37..111
FT /note="YbgF trimerisation"
FT /evidence="ECO:0000259|Pfam:PF16331"
FT REPEAT 216..249
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 105..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 28247 MW; 162FBF3EE3C237EC CRC64;
MSSNFRHHLL SLSLLVGIAA PWAAFAQAPI SSVGSGSVED RVTQLERISN AHSQLLTQLQ
QQLSDNQSDI DSLRGQIQEN QYQLNQVMER QKQIMLQLGS LNNGGAAQPA AGDQSGAATT
ATPAPDAGTA TSGAPVQSGD ANTDYNAAIA LVQDKSRQDD AIVAFQNFIK KYPDSTYQPN
ANYWLGQLNY NKGKKDDAAY YFASVVKNYP KSPKAADAMY KVGVIMQDKG DTAKAKAVYQ
QVINKYPGTD GAKQAQKRLN AM
//
