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Database: UniProt
Entry: A0A1F4HNR0_9BURK
LinkDB: A0A1F4HNR0_9BURK
Original site: A0A1F4HNR0_9BURK 
ID   A0A1F4HNR0_9BURK        Unreviewed;       256 AA.
AC   A0A1F4HNR0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   ORFNames=A3E25_12730 {ECO:0000313|EMBL:OGA99571.1};
OS   Burkholderiales bacterium RIFCSPHIGHO2_12_FULL_69_20.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797561 {ECO:0000313|EMBL:OGA99571.1, ECO:0000313|Proteomes:UP000177017};
RN   [1] {ECO:0000313|EMBL:OGA99571.1, ECO:0000313|Proteomes:UP000177017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGA99571.1}.
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DR   EMBL; MESD01000133; OGA99571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4HNR0; -.
DR   Proteomes; UP000177017; 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   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   NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13174; TPR_6; 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   Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   COILED          53..80
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   256 AA;  27831 MW;  70F40BAF38D73A93 CRC64;
     MALAGVLALS AGGARAGLFD DEEARKAILD LRARIQASDD GASAKIAEQG KAQAALMEQV
     QQLRRSLLDL NTQLEAQRAE SATMRGTQEQ LARDVAEMQR TLKDVSKGQD DRLRALEPQK
     VSLDGKDFLA EPEERRAHDQ AMAALRGGDF DKAATALTTF VQRYPASGYV DSARFWLGNA
     LYGQKNYKEA IAVFRTLVSG APLHPRTPEA LLAVANCQIE MKDMRGARRT IDELTKTYPA
     SEAAVAGKER LGTLKG
//
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