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Database: UniProt
Entry: A0A514EUH2_9ENTR
LinkDB: A0A514EUH2_9ENTR
Original site: A0A514EUH2_9ENTR 
ID   A0A514EUH2_9ENTR        Unreviewed;       262 AA.
AC   A0A514EUH2;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=electrica_03582 {ECO:0000313|EMBL:QDI09663.1};
OS   Klebsiella electrica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1259973 {ECO:0000313|EMBL:QDI09663.1, ECO:0000313|Proteomes:UP000319553};
RN   [1] {ECO:0000313|EMBL:QDI09663.1, ECO:0000313|Proteomes:UP000319553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102253 {ECO:0000313|EMBL:QDI09663.1,
RC   ECO:0000313|Proteomes:UP000319553};
RA   Thiel S., Bunk B., Sproeer C., Overmann J., Jahn D., Biedendieck R.;
RT   "Complete genome sequence of Raoultella electrica 1GB (DSM 102253T),
RT   isolated from anodic biofilms of a glucose-fed microbial fuel cell.";
RL   Submitted (JUN-2019) 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}.
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DR   EMBL; CP041247; QDI09663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A514EUH2; -.
DR   KEGG; ree:electrica_03582; -.
DR   OrthoDB; 9768142at2; -.
DR   Proteomes; UP000319553; 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   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   PANTHER; PTHR37423:SF5; CELL DIVISION COORDINATOR CPOB; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 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.
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..262
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5022276441"
FT   DOMAIN          37..110
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   REGION          106..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   262 AA;  27860 MW;  FC6F591A89BF7BEB CRC64;
     MSSNFRHHLL SLSLLVGIAA PWAAFAQAPI SSVGSGSVED RVTQLERISN AHSQLLTQLQ
     QQLSDNQNDI DSLRGQIQEN QYQLNQVVER QKQILLQIDG LSSGGAAAGA QPSPSAGDQG
     AAATAAPAAS SGAPASSGDA NTDYNAAIAL VKDPSRQDDA QAAFQNFVKK YPDSTYQPNA
     NYWLGQLNYN KGKKDDAAYY FASVVKNYPK SPKAPDAMFK VGVIMQDKGD TAKAKAVYQQ
     VVSKFPGTDG AKQAQKRLNA LG
//
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