ID Q6NAQ7_RHOPA Unreviewed; 345 AA.
AC Q6NAQ7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=RPA1124 {ECO:0000313|EMBL:CAE26567.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE26567.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE26567.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572596; CAE26567.1; -; Genomic_DNA.
DR RefSeq; WP_011156688.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6NAQ7; -.
DR STRING; 258594.RPA1124; -.
DR GeneID; 66892145; -.
DR eggNOG; COG1729; Bacteria.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_044315_0_1_5; -.
DR PhylomeDB; Q6NAQ7; -.
DR Proteomes; UP000001426; Chromosome.
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; 1.20.5.170; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000001426};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 27..345
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009992603"
FT REGION 67..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 36566 MW; 6169CA82C03DF2F1 CRC64;
MSSGFAVSAR SLALMATLAF AAPALAQQYG GEVDPEIRIQ QLEDRLRTLT GQNEELQHRN
RRLEEQVRQL QSGAGAPGAQ QPAPNQATTP PAAPQQPYSQ PAQQPAYGQQ QPGYGQPQAP
MVQPQPAAPQ GGGRRGDAFD PSRDPNAPGV PRALGGGQLP MEQSGGMPAG RAAGAPMDLS
NGNGGYVQGG YPQGGAPSAA KQPPAATAGG ALTTQPPSQT PRDEFDLGIG YMQRRDYALA
EETMRNFAQK YPDNPLTADA QYWLGESFFQ RQMYRDAAEA FLAVTSKHEK SGKAPDALLR
LGQSLSALKE KEAACAALGE IGRKYPQASS SVKKAVDREQ KKLKC
//
