ID A1WGN3_VEREI Unreviewed; 265 AA.
AC A1WGN3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 OrderedLocusNames=Veis_1013 {ECO:0000313|EMBL:ABM56790.1};
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM56790.1, ECO:0000313|Proteomes:UP000000374};
RN [1] {ECO:0000313|Proteomes:UP000000374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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; CP000542; ABM56790.1; -; Genomic_DNA.
DR RefSeq; WP_011808802.1; NC_008786.1.
DR AlphaFoldDB; A1WGN3; -.
DR STRING; 391735.Veis_1013; -.
DR GeneID; 76459690; -.
DR KEGG; vei:Veis_1013; -.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_044315_1_0_4; -.
DR OrthoDB; 8525418at2; -.
DR Proteomes; UP000000374; 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; IPR039565; BamD-like.
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; PF13525; YfiO; 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 Coiled coil {ECO:0000256|HAMAP-Rule:MF_02066};
KW Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW Reference proteome {ECO:0000313|Proteomes:UP000000374};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 31..265
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009990606"
FT DOMAIN 75..128
FT /note="YbgF trimerisation"
FT /evidence="ECO:0000259|Pfam:PF16331"
FT DOMAIN 147..265
FT /note="Outer membrane lipoprotein BamD-like"
FT /evidence="ECO:0000259|Pfam:PF13525"
FT REPEAT 181..214
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 42..118
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ SEQUENCE 265 AA; 29792 MW; D8BAFD4462E8A989 CRC64;
MMPAATMIAA VLRALAAAAL ALALLPAARA ALFEDGEARR AILEMRQRID DLQQSRQRTT
EELRKGADEN AQLRRSLLDL QTQIETLRAE QARLNGQNEQ LRRDLGELQR RQKDITQGVD
ERLRQFEPVK VSVDGREFQA DPAEKRDFEA ALAVFRAGKF ADAGLAFSSF VRQYPRSGFM
PSARFWLGNA QYATREYQEA IVNFRQLLSD TPGHARAPEA ALSIANCQME LKDTRSARKT
LEDLLQAYPQ SEAALAAKER LAYLK
//
