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Database: UniProt
Entry: K8WHV1_9GAMM
LinkDB: K8WHV1_9GAMM
Original site: K8WHV1_9GAMM 
ID   K8WHV1_9GAMM            Unreviewed;       241 AA.
AC   K8WHV1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   ORFNames=OO7_06084 {ECO:0000313|EMBL:EKT59526.1};
OS   Providencia sneebia DSM 19967.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141660 {ECO:0000313|EMBL:EKT59526.1, ECO:0000313|Proteomes:UP000010290};
RN   [1] {ECO:0000313|EMBL:EKT59526.1, ECO:0000313|Proteomes:UP000010290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19967 {ECO:0000313|EMBL:EKT59526.1,
RC   ECO:0000313|Proteomes:UP000010290};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
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:EKT59526.1}.
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DR   EMBL; AKKN01000006; EKT59526.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8WHV1; -.
DR   PATRIC; fig|1141660.3.peg.1229; -.
DR   HOGENOM; CLU_044315_4_0_6; -.
DR   Proteomes; UP000010290; 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   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:UP000010290};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          24..96
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   REPEAT          195..228
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          92..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   241 AA;  25955 MW;  ACF58B5C47666679 CRC64;
     MVGVAVPWTA TAQAPIINVG SGSSSDRLAQ LETAVNSQGQ ILYQIQQQIA DNQRDIDMLR
     GQIQESEYKL NQIVERQKDL YMQLDQAGNG AAASGSATTA DSSSSAPASP AASGGGEKED
     YNAAVTLAMN SKSKAQIDEA IGALQSFIKT YPKSNYQSNA NYWLGQLNYN KGSKDDAAFY
     FATVVKEYPK SQKSSEALYK VGLIMQDKGQ KDKAKAVYQQ VLKQYPNSSG AKLAEKKLSS
     L
//
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