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Database: UniProt
Entry: A0A0P7WFD3_9RHOB
LinkDB: A0A0P7WFD3_9RHOB
Original site: A0A0P7WFD3_9RHOB 
ID   A0A0P7WFD3_9RHOB        Unreviewed;       259 AA.
AC   A0A0P7WFD3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=HLUCCA05_09905 {ECO:0000313|EMBL:KPP92699.1};
OS   Roseibaca calidilacus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Roseibaca.
OX   NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP92699.1, ECO:0000313|Proteomes:UP000050413};
RN   [1] {ECO:0000313|EMBL:KPP92699.1, ECO:0000313|Proteomes:UP000050413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-91 {ECO:0000313|EMBL:KPP92699.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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:KPP92699.1}.
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DR   EMBL; LJSG01000011; KPP92699.1; -; Genomic_DNA.
DR   RefSeq; WP_072245306.1; NZ_FBYC01000004.1.
DR   AlphaFoldDB; A0A0P7WFD3; -.
DR   STRING; 1666912.Ga0058931_0935; -.
DR   OrthoDB; 9763909at2; -.
DR   Proteomes; UP000050413; 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; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
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   SIGNAL          1..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           21..259
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5010392680"
FT   REGION          106..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          23..83
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   259 AA;  27554 MW;  BF95B44AB70E57EA CRC64;
     MRHARAIFVA LCLLAPPAGA DTVAELRAEL GALTGAVADL ARELSSGEAA SQPSYDGSLL
     DRVDRMEAAL ADLTGRTEEL EYRIRRSIDE ASNRLGDLEF RLTELEGGST AGLTPPRLGE
     SATDDDTAQP QLAAGEQQAF DAAMDLAEEG DAEAAATALM QFIETYPGSP LGAEASFKLA
     ETLRTLDRET DAARAYLNLY MTAPDGPEAP RALLALGESL ARLEQVSEAC AMFDELRNRF
     ADSDEAAQSE DARARLACP
//
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