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Database: UniProt
Entry: A0A0W0Z5J2_LEGSP
LinkDB: A0A0W0Z5J2_LEGSP
Original site: A0A0W0Z5J2_LEGSP 
ID   A0A0W0Z5J2_LEGSP        Unreviewed;       300 AA.
AC   A0A0W0Z5J2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=Lspi_1217 {ECO:0000313|EMBL:KTD64410.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD64410.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD64410.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD64410.1,
RC   ECO:0000313|Proteomes:UP000054877};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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:KTD64410.1}.
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DR   EMBL; LNYX01000013; KTD64410.1; -; Genomic_DNA.
DR   RefSeq; WP_058483149.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0Z5J2; -.
DR   STRING; 452.Lspi_1217; -.
DR   PATRIC; fig|452.5.peg.1345; -.
DR   OrthoDB; 9768142at2; -.
DR   Proteomes; UP000054877; 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:UP000054877};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           24..300
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5009985561"
FT   DOMAIN          73..130
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   REPEAT          214..247
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          125..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..110
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   300 AA;  33319 MW;  3E4DCF3E19468FF3 CRC64;
     MKSAQQRLFA LFFCCILAVP AYAEAPVVDD SENFAILDEQ QAAMEQSVAK AQLDDTFDDE
     EIPLAKDDPA DNNDRNAELL DKVQNMKQEI QELRGQVEVL THNLQQLQQQ QLAFYKDLDA
     RLRQGATSQS NQAATQPNTE LSMGSPTDSS TATDSGARHQ NTMAAAVTPT RSNPADEQIS
     YLAAYELVKN KRYDDALTAM QTFVTQYPKG GYTANAQYWL GELYMVKREY NEAIEHFEVV
     LKYFPTSSKA AACSLKIGYA LAASGRQSEA RRRLQQVVKN FPDTPTAQLA VAKLKSLNPS
//
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