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Database: UniProt
Entry: A0A1Y2QCP6_9BURK
LinkDB: A0A1Y2QCP6_9BURK
Original site: A0A1Y2QCP6_9BURK 
ID   A0A1Y2QCP6_9BURK        Unreviewed;       259 AA.
AC   A0A1Y2QCP6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=CAP38_08755 {ECO:0000313|EMBL:OSZ66095.1};
OS   Hydrogenophaga sp. IBVHS2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ66095.1, ECO:0000313|Proteomes:UP000243193};
RN   [1] {ECO:0000313|EMBL:OSZ66095.1, ECO:0000313|Proteomes:UP000243193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ66095.1,
RC   ECO:0000313|Proteomes:UP000243193};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OSZ66095.1}.
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DR   EMBL; NFUT01000002; OSZ66095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2QCP6; -.
DR   STRING; 1985170.CAP38_08755; -.
DR   OrthoDB; 8525418at2; -.
DR   Proteomes; UP000243193; 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; 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.
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:UP000243193};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           32..259
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5013415777"
FT   DOMAIN          67..122
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   DOMAIN          138..259
FT                   /note="Outer membrane lipoprotein BamD-like"
FT                   /evidence="ECO:0000259|Pfam:PF13525"
FT   COILED          71..112
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   259 AA;  28578 MW;  8ED80ADD83618826 CRC64;
     MQAARQRLSG WSGLCAVALS AAVLWPTQAH ALFGDDEARQ AILELRRKVD ANQAASEAAR
     SEGDAATRRS LLELSNQIEQ LRGELARLRG QNEQLAREVA ELQRAQKDVQ AGIDARLREV
     EPLKVELDGQ SFVAQPAEKA QFEAAMATLR RSEFAAASTA YTAFLRQYPA SGYTPSALYW
     LGNAQYAARA YKDSADSHRR LVTEFPNHPR TPEAMLAMAN SQVELKDAKA ARRTLDDLVK
     KYPQSEAAAA AKERLARLR
//
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