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Database: UniProt
Entry: A0A220VEJ3_9GAMM
LinkDB: A0A220VEJ3_9GAMM
Original site: A0A220VEJ3_9GAMM 
ID   A0A220VEJ3_9GAMM        Unreviewed;       260 AA.
AC   A0A220VEJ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE   Flags: Precursor;
GN   Name=ygbF {ECO:0000313|EMBL:ASK78592.1};
GN   Synonyms=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   ORFNames=CF386_06015 {ECO:0000313|EMBL:ASK78592.1};
OS   Paraphotobacterium marinum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Paraphotobacterium.
OX   NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK78592.1, ECO:0000313|Proteomes:UP000242175};
RN   [1] {ECO:0000313|EMBL:ASK78592.1, ECO:0000313|Proteomes:UP000242175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK78592.1,
RC   ECO:0000313|Proteomes:UP000242175};
RX   PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA   Huang Z., Dong C., Shao Z.;
RT   "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT   Vibrionaceae, isolated from surface seawater.";
RL   Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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; CP022355; ASK78592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220VEJ3; -.
DR   KEGG; pmai:CF386_06015; -.
DR   OrthoDB; 9768142at2; -.
DR   Proteomes; UP000242175; Chromosome large.
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; 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   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242175};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           25..260
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5013410559"
FT   DOMAIN          70..115
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   COILED          72..110
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   260 AA;  29208 MW;  DE33AB110CA7CAE5 CRC64;
     MCSHILRRMI VVSIAATATV SAVANSAPVY SAYDTNKNNT SNATQSVYSV TDDSNNESVN
     QPSNNNTYVS SKAQLQLRMQ RNINELQREV DELRGQIQEN NFQIQQLIQQ QKEIAANNKS
     SNSQAPKNAG KDYSNSLQAA SEYNQAIDLI LKKKDFKTAT SKLESFLSKY PNSKYNTNAH
     FWLGQLYYVD KKFSKSLTNF KIVAADSSSS KAPEATYRIA QIYQQKGDKT SEKKYLREVI
     KNYPQSNIAI KAKKDLGLSK
//
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