YIAD_ECOLI
ID YIAD_ECOLI Reviewed; 219 AA.
AC P37665; Q2M7L3; Q6BF24;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable lipoprotein YiaD;
DE Flags: Precursor;
GN Name=yiaD; OrderedLocusNames=b3552, JW5657;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 SEQUENCE REVISION TO 87-88.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX PubMed=2180922; DOI=10.1128/jb.172.4.2194-2198.1990;
RA Pierson D.E., Campbell A.;
RT "Cloning and nucleotide sequence of bisC, the structural gene for biotin
RT sulfoxide reductase in Escherichia coli.";
RL J. Bacteriol. 172:2194-2198(1990).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION, PROBABLE SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF PHE-116; GLY-150; ASP-153; GLY-156; LEU-164 AND ARG-168.
RX PubMed=21228468; DOI=10.1271/bbb.100612;
RA Tachikawa T., Kato J.;
RT "Suppression of the temperature-sensitive mutation of the bamD gene
RT required for the assembly of outer membrane proteins by multicopy of the
RT yiaD gene in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 75:162-164(2011).
RN [8]
RP STRUCTURE BY NMR OF 79-219.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of the folded C-terminal fragment of YiaD from
RT Escherichia coli. Northeast structural genomics consortium target er553.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Suppresses temperature-sensitive mutations in BamB when
CC overexpressed. {ECO:0000269|PubMed:21228468}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Cell outer membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21228468}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M34827; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18529.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48190.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77743.1; -; Genomic_DNA.
DR EMBL; M34827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S47773; S47773.
DR RefSeq; WP_000747625.1; NZ_STEB01000018.1.
DR RefSeq; YP_026228.1; NC_000913.3.
DR PDB; 2K1S; NMR; -; A=79-219.
DR PDB; 2N48; NMR; -; A=79-219.
DR PDBsum; 2K1S; -.
DR PDBsum; 2N48; -.
DR AlphaFoldDB; P37665; -.
DR BMRB; P37665; -.
DR SMR; P37665; -.
DR BioGRID; 4261246; 37.
DR IntAct; P37665; 3.
DR STRING; 511145.b3552; -.
DR TCDB; 9.B.186.1.1; the putative lipoprotein suppressor of a ts bamd mutant, yiad (yiad) family.
DR jPOST; P37665; -.
DR PaxDb; P37665; -.
DR PRIDE; P37665; -.
DR EnsemblBacteria; AAT48190; AAT48190; b3552.
DR EnsemblBacteria; BAE77743; BAE77743; BAE77743.
DR GeneID; 67417196; -.
DR GeneID; 948075; -.
DR KEGG; ecj:JW5657; -.
DR KEGG; eco:b3552; -.
DR PATRIC; fig|1411691.4.peg.3162; -.
DR EchoBASE; EB2180; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016890_6_2_6; -.
DR InParanoid; P37665; -.
DR OMA; IGNYMDK; -.
DR PhylomeDB; P37665; -.
DR BioCyc; EcoCyc:EG12271-MON; -.
DR EvolutionaryTrace; P37665; -.
DR PRO; PR:P37665; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR039567; Gly-zipper.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF13488; Gly-zipper_Omp; 1.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cell outer membrane;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..219
FT /note="Probable lipoprotein YiaD"
FT /id="PRO_0000020134"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..219
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 116
FT /note="F->A: Does not suppress BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT MUTAGEN 150
FT /note="G->A: Partially suppresses BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT MUTAGEN 153
FT /note="D->A: Does not suppress BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT MUTAGEN 156
FT /note="G->A: Does not suppress BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT MUTAGEN 164
FT /note="L->A: Partially suppresses BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT MUTAGEN 168
FT /note="R->A: Does not suppress BamB ts-mutants."
FT /evidence="ECO:0000269|PubMed:21228468"
FT CONFLICT 87..88
FT /note="KL -> NV (in Ref. 1; AAB18529)"
FT /evidence="ECO:0000305"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2K1S"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:2K1S"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2K1S"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2N48"
FT HELIX 158..179
FT /evidence="ECO:0007829|PDB:2K1S"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2K1S"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2K1S"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2K1S"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2K1S"
SQ SEQUENCE 219 AA; 22197 MW; 8EC223021B520418 CRC64;
MKKRVYLIAA VVSGALAVSG CTTNPYTGER EAGKSAIGAG LGSLVGAGIG ALSSSKKDRG
KGALIGAAAG AALGGGVGYY MDVQEAKLRD KMRGTGVSVT RSGDNIILNM PNNVTFDSSS
ATLKPAGANT LTGVAMVLKE YPKTAVNVIG YTDSTGGHDL NMRLSQQRAD SVASALITQG
VDASRIRTQG LGPANPIASN STAEGKAQNR RVEITLSPL
