ID Q20X67_RHOPB Unreviewed; 323 AA.
AC Q20X67;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=RPC_4747 {ECO:0000313|EMBL:ABD90269.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD90269.1};
RN [1] {ECO:0000313|EMBL:ABD90269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD90269.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000301; ABD90269.1; -; Genomic_DNA.
DR AlphaFoldDB; Q20X67; -.
DR STRING; 316056.RPC_4747; -.
DR KEGG; rpc:RPC_4747; -.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_044315_0_1_5; -.
DR OrthoDB; 7185608at2; -.
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 CDD; cd14686; bZIP; 1.
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 Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 27..323
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009992489"
FT REGION 66..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 34008 MW; DF06AA14880E89A3 CRC64;
MSSRFPMFAG GVAMAALLAL SSQAIAQSED IDPEMRVQQL ENQLRTLTGQ NEELQYRNRR
LEEQLKALQS AAPVPGAPPA GYPPANAPPP SVAAAPPAAR APVYDQQPAP LAQDQAGVPP
AAAPAGRRRG DAFDPSQNPG APGVPRALGT TPQSSPVGAP GGRAAGEPLD LNTPRGAPSV
PHGGGPSAGL TTLPPSATPK DEFDLGIGYM QRKDYALAEE TMRNFVKNHP GDPLTADSQY
WLGESFFQRQ LYRDAAEAFL AVTTKYDTSA KAPDALLRLG QSLAALKEKE AACAALGEVT
RKYPRASSGI KQAVDREQKR VKC
//
