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Database: UniProt
Entry: A0A095VMM2_9GAMM
LinkDB: A0A095VMM2_9GAMM
Original site: A0A095VMM2_9GAMM 
ID   A0A095VMM2_9GAMM        Unreviewed;       250 AA.
AC   A0A095VMM2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   ORFNames=HRUBRA_02860 {ECO:0000313|EMBL:KGE02595.1};
OS   Pseudohaliea rubra DSM 19751.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Pseudohaliea.
OX   NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE02595.1, ECO:0000313|Proteomes:UP000029640};
RN   [1] {ECO:0000313|EMBL:KGE02595.1, ECO:0000313|Proteomes:UP000029640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE02595.1,
RC   ECO:0000313|Proteomes:UP000029640};
RX   PubMed=25414506;
RA   Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT   "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT   19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL   Genome Announc. 2:e01208-14(2014).
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:KGE02595.1}.
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DR   EMBL; AUVB01000089; KGE02595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095VMM2; -.
DR   STRING; 1265313.HRUBRA_02860; -.
DR   PATRIC; fig|1265313.6.peg.2816; -.
DR   eggNOG; COG1729; Bacteria.
DR   HOGENOM; CLU_044315_2_1_6; -.
DR   Proteomes; UP000029640; 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   GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR   Gene3D; 1.20.5.110; -; 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   InterPro; IPR032519; YbgF_tri.
DR   NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR   Pfam; PF16331; TolA_bind_tri; 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   Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          42..99
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   REPEAT          203..236
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   250 AA;  27575 MW;  5C7856BB1AE7499A CRC64;
     MEAERARSGS PTTAQPALAR SYGLDSSAGP ATVSRPPAPA SNSEETIGNL FIQLQRLQQE
     VMQLNGKVEE QAYELRRLKE QSLERYLDLD RRLAGSGAPT SGNTGESTVI GMPDAGSGAE
     AAEQPGEGDA YRAAYARVRN QEFDAAVAAF KQFLERFPDG RYAPNAHYWL GELYLVLQPP
     DPEAARQSFM LLLDQYPGNS KEPDALYKLG RVHYIKGNRE RSREFMDRVL RQYPDSSAAG
     LAGEFIDQNL
//
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