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Database: UniProt
Entry: A0A1H4BCJ4_9GAMM
LinkDB: A0A1H4BCJ4_9GAMM
Original site: A0A1H4BCJ4_9GAMM 
ID   A0A1H4BCJ4_9GAMM        Unreviewed;       271 AA.
AC   A0A1H4BCJ4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
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=SAMN02745729_103251 {ECO:0000313|EMBL:SEA45542.1};
OS   Marinobacterium iners DSM 11526.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1122198 {ECO:0000313|EMBL:SEA45542.1, ECO:0000313|Proteomes:UP000242469};
RN   [1] {ECO:0000313|Proteomes:UP000242469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11526 {ECO:0000313|Proteomes:UP000242469};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNRJ01000003; SEA45542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4BCJ4; -.
DR   STRING; 1122198.SAMN02745729_103251; -.
DR   OrthoDB; 9768142at2; -.
DR   Proteomes; UP000242469; 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   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:UP000242469};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           23..271
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5017490327"
FT   DOMAIN          54..107
FT                   /note="YbgF trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF16331"
FT   REPEAT          187..220
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   COILED          63..97
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   271 AA;  29464 MW;  18126CC4814BEF24 CRC64;
     MKSAATAKAT ILLVLASSWS YAAPVPVIEI TETPVVPRTG GTQPLQVQSA AGYSVQNELL
     FSLQQLQDEV RMLRGALEEQ QHKVERLEQQ QRERYRDMDR RISLLMSAVP DDALLAAQGN
     PEQPKQAAGL PNVTDNAELN ASVEGVAAGD AAAYDKAYSH VRQREFDQAE KSFELFLNDY
     PNSSLVPNAW YWLGEVKLAQ GKVEAATSAF NQVVTGYPGH AKAADALYKL GVLSERGGDG
     AAARALMKRV QDEYPQTSAA GLARSFLSNQ Q
//
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