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Database: UniProt
Entry: A0A1T4VIU1_9GAMM
LinkDB: A0A1T4VIU1_9GAMM
Original site: A0A1T4VIU1_9GAMM 
ID   A0A1T4VIU1_9GAMM        Unreviewed;       263 AA.
AC   A0A1T4VIU1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN02745213_01582 {ECO:0000313|EMBL:SKA64869.1};
OS   Succinivibrio dextrinosolvens DSM 3072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Succinivibrionaceae; Succinivibrio.
OX   NCBI_TaxID=1123324 {ECO:0000313|EMBL:SKA64869.1, ECO:0000313|Proteomes:UP000242432};
RN   [1] {ECO:0000313|Proteomes:UP000242432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3072 {ECO:0000313|Proteomes:UP000242432};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) 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; FUXX01000027; SKA64869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4VIU1; -.
DR   STRING; 83771.SAMN02910357_00315; -.
DR   Proteomes; UP000242432; 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   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   NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF90257; Myosin rod fragments; 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:UP000242432};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           32..263
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5013410836"
FT   REPEAT          217..250
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   COILED          33..88
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   263 AA;  28667 MW;  153136EC886AFED1 CRC64;
     MNKFYSLSKR SFAISLILSA FVFINSAYAD AQTDSMQRAM LNMQNQIQQL QDKLAESQGQ
     IEELNHEKKI LAAENEKLKA QISQMAANTP AASAATAENT NGNTDGTSQA VTMKTETGGA
     TATLSPAKKG TVAKANLPAV PADAQKLYQD SYALLNKGDL DAAAKGFKSY TSKYSNNALT
     PNAWYWLGQI QYKQNKFQDA RISFLNTAKF KDSDKRADAL YKLGVTSKAL GDKEKAKKFF
     DVLIKTYPTA SSSALAKKEL QSL
//
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