ID A0A433JLD4_9GAMM Unreviewed; 307 AA.
AC A0A433JLD4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE Flags: Precursor;
GN Name=ybgF {ECO:0000313|EMBL:RUQ90068.1};
GN Synonyms=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN ORFNames=EKM59_02735 {ECO:0000313|EMBL:RUQ90068.1};
OS Legionella septentrionalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=2498109 {ECO:0000313|EMBL:RUQ90068.1, ECO:0000313|Proteomes:UP000288012};
RN [1] {ECO:0000313|EMBL:RUQ90068.1, ECO:0000313|Proteomes:UP000288012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=km714 {ECO:0000313|Proteomes:UP000288012};
RA Wu H.;
RT "Legionella sp,whole genome shotgun sequence.";
RL Submitted (DEC-2018) 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}.
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:RUQ90068.1}.
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DR EMBL; RZGR01000005; RUQ90068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433JLD4; -.
DR Proteomes; UP000288012; 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 SMART; SM00028; TPR; 2.
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:UP000288012};
KW Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT CHAIN 22..307
FT /note="Cell division coordinator CpoB"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT /id="PRO_5019593713"
FT DOMAIN 75..130
FT /note="YbgF trimerisation"
FT /evidence="ECO:0000259|Pfam:PF16331"
FT REPEAT 222..255
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 125..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..109
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT COMPBIAS 128..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 33946 MW; 0C63CBC47CA00427 CRC64;
MIKSRFLLAA CLSCFLIPSF AAAPVIDDSE NFMLLEEQQD AYEQPVARAP VEIYDNDDEP
ALAYDTAEPH NRNDNSMLLA KIQGLQQEIQ ELRGQLEIQT HDLKLLQQQQ LTFYKDLDER
IRNAAAQQAQ KAPAQLSVKE LSEKQPSPHL STPTAQAPKA PTANAPAIVK SQPANAASRH
NPADEQISYL AAYELVKNKK YDGALTAMQN FVNQYPQGGY TANAQYWLGE LYMVKKNYSQ
AISHFEAVLQ QFPSSSKSAA SLLKIGYALA ASGKKTEAKQ RLQEVIKNYP DTNTAQLATA
KLETLGS
//
