YTFB_ECOLI
ID YTFB_ECOLI Reviewed; 212 AA.
AC P39310; Q2M699;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cell division protein YtfB {ECO:0000305};
GN Name=ytfB; OrderedLocusNames=b4206, JW5745;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP OVEREXPRESSION.
RX PubMed=29686141; DOI=10.1128/jb.00046-18;
RA Jorgenson M.A., Young K.D.;
RT "YtfB, an OapA domain-containing protein, is a new cell division protein in
RT Escherichia coli.";
RL J. Bacteriol. 200:E00046-E00046(2018).
CC -!- FUNCTION: Cell division protein whose function is related to the
CC generation of a transient cell wall structure. Function is linked to
CC the late stages of cell division. {ECO:0000269|PubMed:29686141}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the septal ring prior
CC to the onset of constriction and remains at the midcell throughout
CC cytokinesis. Recruitment to the septal ring requires FtsZ, but not
CC downstream division proteins. {ECO:0000269|PubMed:29686141}.
CC -!- DOMAIN: The OapA domain binds peptidoglycan.
CC {ECO:0000269|PubMed:29686141}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene has no discernible impact on
CC morphology or cell size. YtfB/dedD double mutant grows as filamentous
CC cells. {ECO:0000269|PubMed:29686141}.
CC -!- MISCELLANEOUS: Overproduction causes cells to filament, most likely by
CC disrupting FtsZ ring assembly. {ECO:0000269|PubMed:29686141}.
CC -!- SIMILARITY: Belongs to the OapA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97102.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97102.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77163.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78207.1; -; Genomic_DNA.
DR PIR; S56431; S56431.
DR RefSeq; NP_418627.4; NC_000913.3.
DR RefSeq; WP_001119478.1; NZ_SSZK01000013.1.
DR AlphaFoldDB; P39310; -.
DR SMR; P39310; -.
DR BioGRID; 4259638; 396.
DR BioGRID; 853019; 2.
DR IntAct; P39310; 2.
DR STRING; 511145.b4206; -.
DR jPOST; P39310; -.
DR PaxDb; P39310; -.
DR PRIDE; P39310; -.
DR EnsemblBacteria; AAC77163; AAC77163; b4206.
DR EnsemblBacteria; BAE78207; BAE78207; BAE78207.
DR GeneID; 66671874; -.
DR GeneID; 948727; -.
DR KEGG; ecj:JW5745; -.
DR KEGG; eco:b4206; -.
DR PATRIC; fig|1411691.4.peg.2495; -.
DR EchoBASE; EB2395; -.
DR eggNOG; COG3061; Bacteria.
DR HOGENOM; CLU_065360_1_0_6; -.
DR OMA; QQWRTYR; -.
DR PhylomeDB; P39310; -.
DR BioCyc; EcoCyc:G7864-MON; -.
DR PRO; PR:P39310; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IDA:EcoCyc.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IBA:GO_Central.
DR InterPro; IPR013731; OapA_N.
DR InterPro; IPR007340; Opacity-associatedA.
DR Pfam; PF04225; OapA; 1.
DR Pfam; PF08525; OapA_N; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..212
FT /note="Cell division protein YtfB"
FT /id="PRO_0000169822"
FT TRANSMEM 34..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 88..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..212
FT /note="OapA"
FT /evidence="ECO:0000305|PubMed:29686141"
FT COMPBIAS 105..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 23505 MW; 7E475BDE4933A164 CRC64;
MPGRFELKPT LEKVWHAPDN FRFMDPLPPM HRRGIIIAAI VLVVGFLLPS DDTPNAPVVT
REAQLDIQSQ SQPPTEEQLR AQLVTPQNDP DQVAPVAPEP IQEGQPEEQP QTTQTQPFQP
DSGIDNQWRS YRVEPGKTMA QLFRDHGLPA TDVYAMAQVE GAGKPLSNLQ NGQMVKIRQN
ASGVVTGLTI DTGNNQQVLF TRQPDGSFIR AR
