CPOB_ECOLI
ID CPOB_ECOLI Reviewed; 263 AA.
AC P45955; P75756;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cell division coordinator CpoB {ECO:0000255|HAMAP-Rule:MF_02066, ECO:0000305};
DE Flags: Precursor;
GN Name=cpoB {ECO:0000255|HAMAP-Rule:MF_02066, ECO:0000303|PubMed:25951518};
GN Synonyms=ybgF; OrderedLocusNames=b0742, JW0732;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1574003; DOI=10.1111/j.1365-2958.1992.tb01523.x;
RA Lazzaroni J.-C., Portalier R.;
RT "The excC gene of Escherichia coli K-12 required for cell envelope
RT integrity encodes the peptidoglycan-associated lipoprotein (PAL).";
RL Mol. Microbiol. 6:735-742(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [6]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=8763928; DOI=10.1128/jb.178.14.4031-4038.1996;
RA Vianney A., Muller M.M., Clavel T., Lazzaroni J.C., Portalier R.,
RA Webster R.E.;
RT "Characterization of the tol-pal region of Escherichia coli K-12:
RT translational control of tolR expression by TolQ and identification of a
RT new open reading frame downstream of pal encoding a periplasmic protein.";
RL J. Bacteriol. 178:4031-4038(1996).
RN [7]
RP INTERACTION WITH TOLA.
RX PubMed=11994151; DOI=10.1046/j.1365-2958.2002.02895.x;
RA Walburger A., Lazdunski C., Corda Y.;
RT "The Tol/Pal system function requires an interaction between the C-terminal
RT domain of TolA and the N-terminal domain of TolB.";
RL Mol. Microbiol. 44:695-708(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBSTRATE FOR SECB.
RC STRAIN=K12 / MC4100;
RX PubMed=16352602; DOI=10.1074/jbc.m509929200;
RA Baars L., Ytterberg A.J., Drew D., Wagner S., Thilo C., van Wijk K.J.,
RA de Gier J.W.;
RT "Defining the role of the Escherichia coli chaperone SecB using comparative
RT proteomics.";
RL J. Biol. Chem. 281:10024-10034(2006).
RN [9]
RP SUBUNIT, DOMAIN, TPR REPEATS, AND MUTAGENESIS OF TYR-173; PRO-211 AND
RP TYR-247.
RC STRAIN=MG1566;
RX PubMed=20455268; DOI=10.1002/prot.22726;
RA Krachler A.M., Sharma A., Kleanthous C.;
RT "Self-association of TPR domains: Lessons learned from a designed,
RT consensus-based TPR oligomer.";
RL Proteins 78:2131-2143(2010).
RN [10]
RP FUNCTION, INTERACTION WITH PBP1B AND TOLA, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25951518; DOI=10.7554/elife.07118;
RA Gray A.N., Egan A.J., Van't Veer I.L., Verheul J., Colavin A.,
RA Koumoutsi A., Biboy J., Altelaar A.F., Damen M.J., Huang K.C.,
RA Simorre J.P., Breukink E., den Blaauwen T., Typas A., Gross C.A.,
RA Vollmer W.;
RT "Coordination of peptidoglycan synthesis and outer membrane constriction
RT during Escherichia coli cell division.";
RL Elife 4:E07118-E07118(2015).
RN [11] {ECO:0007744|PDB:2WZ7, ECO:0007744|PDB:2XDJ}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 35-109, SUBUNIT, INTERACTION WITH
RP TOLA, AND DOMAIN.
RX PubMed=20816983; DOI=10.1016/j.jmb.2010.08.050;
RA Krachler A.M., Sharma A., Cauldwell A., Papadakos G., Kleanthous C.;
RT "TolA modulates the oligomeric status of YbgF in the bacterial periplasm.";
RL J. Mol. Biol. 403:270-285(2010).
CC -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and outer
CC membrane constriction during cell division. Promotes physical and
CC functional coordination of the PBP1B-LpoB and Tol machines, and
CC regulates PBP1B activity in response to Tol energy state.
CC {ECO:0000269|PubMed:25951518}.
CC -!- SUBUNIT: Homotrimer (PubMed:20455268, PubMed:20816983). Interacts
CC directly with the central domain of TolA and with PBP1B
CC (PubMed:11994151, PubMed:20816983, PubMed:25951518). Binding to TolA
CC disrupts the homotrimer to form a YbgF/TolA heterodimer with weak
CC affinity (PubMed:20816983). Forms a quaternary complex with PBP1B-LpoB
CC and TolA (PubMed:25951518). {ECO:0000269|PubMed:11994151,
CC ECO:0000269|PubMed:20455268, ECO:0000269|PubMed:20816983,
CC ECO:0000269|PubMed:25951518}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02066,
CC ECO:0000269|PubMed:8763928}. Note=Targeting to the Sec-translocase for
CC transport across the inner membrane is SecB-dependent
CC (PubMed:16352602). Localizes to the septum concurrent with PBP1B-LpoB
CC and Tol at the onset of constriction (PubMed:25951518). Localization is
CC dependent on divisome assembly and requires ongoing septal
CC peptidoglycan synthesis (PubMed:25951518).
CC {ECO:0000269|PubMed:16352602, ECO:0000269|PubMed:25951518}.
CC -!- DOMAIN: Contains an N-terminal coiled-coil domain and a C-terminal TPR
CC domain, separated by a flexible linker. The N-terminal domain forms a
CC stable trimer and controls the oligomeric status. The C-terminal
CC domain, which can also trimerize, is involved in interaction with TolA.
CC {ECO:0000269|PubMed:20455268, ECO:0000269|PubMed:20816983}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is sensitive to multiple beta-
CC lactams, including cefsulodin. It leads to defects in outer membrane
CC integrity, envelope defects and elevated cell lysis.
CC {ECO:0000269|PubMed:25951518}.
CC -!- SIMILARITY: Belongs to the CpoB family. {ECO:0000255|HAMAP-
CC Rule:MF_02066, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X65796; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X65796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC73836.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35408.1; -; Genomic_DNA.
DR PIR; E64810; E64810.
DR RefSeq; NP_415270.1; NC_000913.3.
DR RefSeq; WP_000097571.1; NZ_SSZK01000033.1.
DR PDB; 2WZ7; X-ray; 2.48 A; A/B/C/D/E/F=35-109.
DR PDB; 2XDJ; X-ray; 1.82 A; A/B/C/D/E/F=35-109.
DR PDB; 6G5S; NMR; -; A=139-263.
DR PDBsum; 2WZ7; -.
DR PDBsum; 2XDJ; -.
DR PDBsum; 6G5S; -.
DR AlphaFoldDB; P45955; -.
DR SMR; P45955; -.
DR BioGRID; 4260725; 202.
DR BioGRID; 851559; 2.
DR DIP; DIP-11392N; -.
DR IntAct; P45955; 3.
DR STRING; 511145.b0742; -.
DR TCDB; 2.C.1.2.1; the tonb-exbb-exbd/tola-tolq-tolr outer membrane receptor energizers and stabilizers (tonb/tola) family.
DR jPOST; P45955; -.
DR PaxDb; P45955; -.
DR PRIDE; P45955; -.
DR EnsemblBacteria; AAC73836; AAC73836; b0742.
DR EnsemblBacteria; BAA35408; BAA35408; BAA35408.
DR GeneID; 947227; -.
DR KEGG; ecj:JW0732; -.
DR KEGG; eco:b0742; -.
DR PATRIC; fig|1411691.4.peg.1530; -.
DR EchoBASE; EB2698; -.
DR eggNOG; COG1729; Bacteria.
DR HOGENOM; CLU_044315_4_0_6; -.
DR InParanoid; P45955; -.
DR OMA; YWLGEVN; -.
DR PhylomeDB; P45955; -.
DR BioCyc; EcoCyc:EG12854-MON; -.
DR BioCyc; MetaCyc:EG12854-MON; -.
DR EvolutionaryTrace; P45955; -.
DR PRO; PR:P45955; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IDA:EcoCyc.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0070206; P:protein trimerization; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 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 Pfam; PF16331; TolA_bind_tri; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR02795; tol_pal_ybgF; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Periplasm;
KW Reference proteome; Repeat; Signal; TPR repeat.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..263
FT /note="Cell division coordinator CpoB"
FT /id="PRO_0000013804"
FT REPEAT 143..176
FT /note="TPR 1"
FT /evidence="ECO:0000305|PubMed:20455268"
FT REPEAT 180..213
FT /note="TPR 2"
FT /evidence="ECO:0000305|PubMed:20455268"
FT REPEAT 217..250
FT /note="TPR 3"
FT /evidence="ECO:0000305|PubMed:20455268"
FT REGION 106..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02066"
FT COMPBIAS 106..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 173
FT /note="Y->D: Decreases self-association."
FT /evidence="ECO:0000269|PubMed:20455268"
FT MUTAGEN 211
FT /note="P->D: Does not affect oligomerization."
FT /evidence="ECO:0000269|PubMed:20455268"
FT MUTAGEN 247
FT /note="Y->D: Forms dimers instead of trimers."
FT /evidence="ECO:0000269|PubMed:20455268"
FT CONFLICT 224
FT /note="G -> A (in Ref. 1; X65796)"
FT /evidence="ECO:0000305"
FT HELIX 38..99
FT /evidence="ECO:0007829|PDB:2XDJ"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:6G5S"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:6G5S"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6G5S"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:6G5S"
SQ SEQUENCE 263 AA; 28231 MW; EE9845C0A8E803A2 CRC64;
MSSNFRHQLL SLSLLVGIAA PWAAFAQAPI SSVGSGSVED RVTQLERISN AHSQLLTQLQ
QQLSDNQSDI DSLRGQIQEN QYQLNQVVER QKQILLQIDS LSSGGAAAQS TSGDQSGAAA
STTPTADAGT ANAGAPVKSG NANTDYNAAI ALVQDKSRQD DAMVAFQNFI KNYPDSTYLP
NANYWLGQLN YNKGKKDDAA YYFASVVKNY PKSPKAADAM FKVGVIMQDK GDTAKAKAVY
QQVISKYPGT DGAKQAQKRL NAM
