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Database: UniProt
Entry: P0A131
LinkDB: P0A131
Original site: P0A131 
ID   CPOB_PSEPU              Reviewed;         268 AA.
AC   P0A131; P43037;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000255|HAMAP-Rule:MF_02066};
DE   AltName: Full=ORF2;
DE   Flags: Precursor;
GN   Name=cpoB {ECO:0000255|HAMAP-Rule:MF_02066};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=8626299; DOI=10.1128/jb.178.6.1699-1706.1996;
RA   Rodriguez-Herva J.J., Ramos-Gonzalez M.I., Ramos J.L.;
RT   "The Pseudomonas putida peptidoglycan-associated outer membrane lipoprotein
RT   is involved in maintenance of the integrity of the cell cell envelope.";
RL   J. Bacteriol. 178:1699-1706(1996).
CC   -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and outer
CC       membrane constriction during cell division. {ECO:0000255|HAMAP-
CC       Rule:MF_02066}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02066}.
CC   -!- DOMAIN: Contains an N-terminal coiled-coil domain and a C-terminal TPR
CC       domain, separated by a flexible linker. {ECO:0000250|UniProtKB:P45955}.
CC   -!- SIMILARITY: Belongs to the CpoB family. {ECO:0000255|HAMAP-
CC       Rule:MF_02066}.
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DR   EMBL; X74218; CAA52295.1; -; Genomic_DNA.
DR   RefSeq; WP_003254754.1; NZ_SPUU01000024.1.
DR   AlphaFoldDB; P0A131; -.
DR   SMR; P0A131; -.
DR   GeneID; 83678590; -.
DR   eggNOG; COG1729; Bacteria.
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; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Periplasm; Repeat; Signal;
KW   TPR repeat.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..268
FT                   /note="Cell division coordinator CpoB"
FT                   /id="PRO_0000013806"
FT   REPEAT          149..181
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000250|UniProtKB:P45955"
FT   REPEAT          185..218
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000250|UniProtKB:P45955"
FT   REPEAT          222..255
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000250|UniProtKB:P45955"
FT   REGION          104..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          58..94
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   268 AA;  28730 MW;  3183F1F06B1E2A21 CRC64;
     MRMCRRVVTV LALSLPLAAW AEVPVVDDNA GSYPPAGYGT SGAYAGSGAS APASAQGQLF
     MQLQQMQDQL SRQQGIIEEL QNDVSRMKQE NLERYQDLDR RINSGAAPAA TPDNSSGGGA
     SNAAPDAAAG AAAQQPAGSS QPGDPAKEKL YYDAAFDLIK QKDFDKASQA FNAFLRKYPN
     SQYAGNAQYW LGEVNLAKGD LQGASQAFAQ VSQKYPKHSK VPDSLYKLAD VERRMGHTDK
     VKGILQQVVT QYPGTSAAQL AQRDLQKL
//
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