ID H0C3L5_9BURK Unreviewed; 263 AA.
AC H0C3L5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=KYG_21709 {ECO:0000313|EMBL:EHL20836.1};
OS Acidovorax sp. NO-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL20836.1, ECO:0000313|Proteomes:UP000003485};
RN [1] {ECO:0000313|EMBL:EHL20836.1, ECO:0000313|Proteomes:UP000003485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL20836.1,
RC ECO:0000313|Proteomes:UP000003485};
RX PubMed=22374962; DOI=10.1128/JB.06814-11;
RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL J. Bacteriol. 194:1635-1636(2012).
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; AGTS01000145; EHL20836.1; -; Genomic_DNA.
DR RefSeq; WP_008906952.1; NZ_AGTS01000145.1.
DR AlphaFoldDB; H0C3L5; -.
DR STRING; 512030.KYG_21709; -.
DR PATRIC; fig|512030.4.peg.4270; -.
DR OrthoDB; 8525418at2; -.
DR Proteomes; UP000003485; 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; 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:UP000003485};
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..263
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009991732"
FT DOMAIN 61..127
FT /note="YbgF trimerisation"
FT /evidence="ECO:0000259|Pfam:PF16331"
FT DOMAIN 146..263
FT /note="Outer membrane lipoprotein BamD-like"
FT /evidence="ECO:0000259|Pfam:PF13525"
FT REPEAT 179..212
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 47..109
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ SEQUENCE 263 AA; 29363 MW; C579F2A388D319D4 CRC64;
MRSAVVGFPV KTLAMAALLA ATLSSAHAAI FEDGEARRAI LEMRQRVDGL QASQQRSSDE
LRKLAEENAQ LRRGLLDLQT QIESLRADKA RLHGQNEQLL RDVGELQRRQ KDIAQGVDER
LRQFEPVTVT VDGREFQADP SEKRDFDSAL AVFRSGKFAE SGNAFSAFLR QYPRSGYAPS
ARFWLGNAQY ATRDYKGAIG NFRQMLSDAP DHARAPEAAL SIANCQIELK ETRTARKTLE
DLVRAYPQSE AAVAAKERLS RLK
//
