ID D0YYR9_PHODD Unreviewed; 244 AA.
AC D0YYR9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE Flags: Precursor;
GN Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN ORFNames=VDA_002432 {ECO:0000313|EMBL:EEZ41400.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ41400.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ41400.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ41400.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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; ADBS01000001; EEZ41400.1; -; Genomic_DNA.
DR RefSeq; WP_005300080.1; NZ_ADBS01000001.1.
DR AlphaFoldDB; D0YYR9; -.
DR eggNOG; COG1729; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
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 Pfam; PF16331; TolA_bind_tri; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 29..244
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009991134"
FT DOMAIN 29..100
FT /note="YbgF trimerisation"
FT /evidence="ECO:0000259|Pfam:PF16331"
FT REPEAT 160..193
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 196..229
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 89..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 244 AA; 27362 MW; 960DB2951E076C9C CRC64;
MNSNNMRKLA LGLLVGAATQ LVAVPAFADS QLDRLERMLD ARNQMMLDMQ RQLDQISTDV
DDLRGKVERN SYDLKQMLER QRELYREVDT LSSQQAQQAK ETKATNTDAK ENQESYSSNL
DENQAYEKAV NLILKEKDYQ GATKAFNDFI ATYPKSVYAP NAHYWLGQLY FAQGQMKAAD
EHFTAVVAAK DSSKRADALL KLGAIAQKAN DNAKATQYYQ QVVKEFPSST TATQAQAALN
KLGQ
//
