YEBF_ECOLI
ID YEBF_ECOLI Reviewed; 118 AA.
AC P33219;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein YebF {ECO:0000305};
DE Flags: Precursor;
GN Name=yebF; OrderedLocusNames=b1847, JW1836;
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;
RA Smith J.M., Nygaard P.;
RT "Purine and one-carbon metabolism in Escherichia coli K12: DNA sequence of
RT a second GAR transformylase.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 PROTEIN SEQUENCE OF 22-31, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=16369539; DOI=10.1038/nbt1174;
RA Zhang G., Brokx S., Weiner J.H.;
RT "Extracellular accumulation of recombinant proteins fused to the carrier
RT protein YebF in Escherichia coli.";
RL Nat. Biotechnol. 24:100-104(2006).
RN [6] {ECO:0007744|PDB:2LQV}
RP STRUCTURE BY NMR OF 22-118, DISULFIDE BOND, SUBUNIT, INTERACTION WITH OMPF
RP AND OMPC, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-35;
RP 58-ARG--ASP-62; LYS-64; VAL-66; 78-GLN-ASP-79; 85-ASP-LYS-86; THR-92 AND
RP CYS-108.
RX PubMed=22658749; DOI=10.1016/j.str.2012.04.014;
RA Prehna G., Zhang G., Gong X., Duszyk M., Okon M., McIntosh L.P.,
RA Weiner J.H., Strynadka N.C.;
RT "A protein export pathway involving Escherichia coli porins.";
RL Structure 20:1154-1166(2012).
CC -!- SUBUNIT: Monomer in solution (PubMed:22658749). Interacts with
CC OmpF/OmpC at the periplasmic face of the membrane (PubMed:22658749).
CC {ECO:0000269|PubMed:22658749}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16369539}. Note=The
CC outer membrane proteins OmpF, OmpC and OmpX are involved in YebF
CC export. OmpX may help target and load YebF onto the OmpF/OmpC porins.
CC {ECO:0000269|PubMed:22658749}.
CC -!- DOMAIN: Contains an ordered core and an extensive dynamic surface
CC formed by two regions, dynamic loop1 and dynamic loop2. The core is
CC stabilized by a disulfide and ressembles the cystatin family.
CC {ECO:0000269|PubMed:22658749}.
CC -!- SIMILARITY: Belongs to the YebF family. {ECO:0000255|HAMAP-
CC Rule:MF_01435, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA15653.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L20897; AAA23859.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74917.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15653.1; ALT_INIT; Genomic_DNA.
DR PIR; G64946; G64946.
DR RefSeq; NP_416361.2; NC_000913.3.
DR RefSeq; WP_001350516.1; NZ_LN832404.1.
DR PDB; 2LQV; NMR; -; A=22-118.
DR PDBsum; 2LQV; -.
DR AlphaFoldDB; P33219; -.
DR BMRB; P33219; -.
DR SMR; P33219; -.
DR BioGRID; 4263507; 4.
DR STRING; 511145.b1847; -.
DR jPOST; P33219; -.
DR PaxDb; P33219; -.
DR PRIDE; P33219; -.
DR EnsemblBacteria; AAC74917; AAC74917; b1847.
DR EnsemblBacteria; BAA15653; BAA15653; BAA15653.
DR GeneID; 946363; -.
DR KEGG; ecj:JW1836; -.
DR KEGG; eco:b1847; -.
DR PATRIC; fig|1411691.4.peg.402; -.
DR EchoBASE; EB1755; -.
DR eggNOG; ENOG5031MN2; Bacteria.
DR HOGENOM; CLU_161319_1_0_6; -.
DR PhylomeDB; P33219; -.
DR BioCyc; EcoCyc:EG11807-MON; -.
DR PRO; PR:P33219; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 3.10.450.300; -; 1.
DR HAMAP; MF_01435; YebF; 1.
DR InterPro; IPR020236; Uncharacterised_YebF.
DR InterPro; IPR038703; YebF/Cmi_sf.
DR InterPro; IPR025603; YebF/ColM_immunity.
DR Pfam; PF13995; YebF; 1.
DR PROSITE; PS51979; YEBF_CMI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:16369539"
FT CHAIN 22..118
FT /note="Protein YebF"
FT /id="PRO_0000045946"
FT DOMAIN 31..118
FT /note="YebF/Cmi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01323"
FT REGION 53..74
FT /note="Dynamic loop1"
FT /evidence="ECO:0000305|PubMed:22658749"
FT REGION 91..103
FT /note="Dynamic loop2"
FT /evidence="ECO:0000305|PubMed:22658749"
FT DISULFID 35..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01323,
FT ECO:0000269|PubMed:22658749, ECO:0007744|PDB:2LQV"
FT MUTAGEN 35
FT /note="C->A: Lack of YebF secretion."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 58..62
FT /note="RWADD->AAADA: 90% reduction in levels of YebF
FT secretion."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 64
FT /note="K->A: 80% reduction in levels of YebF secretion;
FT when associated with A-66 and A-92."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 66
FT /note="V->A: 80% reduction in levels of YebF secretion;
FT when associated with A-64 and A-92."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 78..79
FT /note="QD->AA: Slight decrease in levels of YebF
FT secretion."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 85..86
FT /note="DK->AA: Slight decrease in levels of YebF
FT secretion."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 92
FT /note="T->A: 80% reduction in levels of YebF secretion;
FT when associated with A-64 and A-66."
FT /evidence="ECO:0000269|PubMed:22658749"
FT MUTAGEN 108
FT /note="C->A: Lack of YebF secretion."
FT /evidence="ECO:0000269|PubMed:22658749"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2LQV"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:2LQV"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2LQV"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2LQV"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2LQV"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2LQV"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2LQV"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:2LQV"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2LQV"
SQ SEQUENCE 118 AA; 12962 MW; 8C84A35F882DCE9E CRC64;
MKKRGAFLGL LLVSACASVF AANNETSKSV TFPKCEDLDA AGIAASVKRD YQQNRVARWA
DDQKIVGQAD PVAWVSLQDI QGKDDKWSVP LTVRGKSADI HYQVSVDCKA GMAEYQRR
