ID S9QH33_9RHOB Unreviewed; 272 AA.
AC S9QH33;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 48.
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=thalar_00991 {ECO:0000313|EMBL:EPX80771.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX80771.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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:EPX80771.1}.
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DR EMBL; AONI01000008; EPX80771.1; -; Genomic_DNA.
DR AlphaFoldDB; S9QH33; -.
DR STRING; 1123360.thalar_00991; -.
DR PATRIC; fig|1123360.3.peg.981; -.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_997073_0_0_5; -.
DR OrthoDB; 9763909at2; -.
DR Proteomes; UP000015351; 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.
DR PROSITE; PS50005; TPR; 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:UP000015351};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 20..272
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5009992841"
FT REPEAT 186..219
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT COILED 24..90
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ SEQUENCE 272 AA; 28450 MW; 59416B8FAE2FDD3D CRC64;
MRKVLMCLSF ALSVGPLAAQ DSSLADIRAE LGQLNGAIVQ LRSELSGGNT GGLTITGDTL
QRIDIIEAAL ARLTSKTEDL ENRINRVVTD GTNRVGDLEF RLCELEEGCD LGSIGETPLL
GGGDASSAPV AVAPNTTPDA GGAELAVSEK ADYERAQEAL AAGDFRGAAD KFAAFNESYP
GGPLAADAHF LRGQALAELG DWNNAARAYL ESFSGSPDAP RAPEALYRLG LALHKLGQSQ
EGCLMLQEVG VRYPGSDQVL PANSSMRELG CQ
//
