YIHG_ECOLI
ID YIHG_ECOLI Reviewed; 310 AA.
AC P32129; Q2M8G0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable acyltransferase YihG;
DE EC=2.3.-.-;
GN Name=yihG; OrderedLocusNames=b3862, JW3834;
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=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 PRELIMINARY FUNCTION, AND INDUCTION.
RX PubMed=8876178; DOI=10.1073/pnas.93.21.11580;
RA Cao G.J., Pogliano J., Sarkar N.;
RT "Identification of the coding region for a second poly(A) polymerase in
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11580-11585(1996).
RN [5]
RP SHOWS THAT THIS IS NOT POLY(A) POLYMERASE II.
RX PubMed=10594834; DOI=10.1046/j.1365-2958.1999.01674.x;
RA Mohanty B.K., Kushner S.R.;
RT "Residual polyadenylation in poly(A) polymerase I (pcnB) mutants of
RT Escherichia coli does not result from the activity encoded by the f310
RT gene.";
RL Mol. Microbiol. 34:1109-1119(1999).
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).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: In stationary phase. {ECO:0000269|PubMed:8876178}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a poly(A) polymerase II.
CC {ECO:0000305|PubMed:8876178}.
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DR EMBL; L19201; AAB02997.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76860.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77446.1; -; Genomic_DNA.
DR PIR; S40808; S40808.
DR RefSeq; NP_418299.1; NC_000913.3.
DR RefSeq; WP_001311257.1; NZ_SSZK01000026.1.
DR AlphaFoldDB; P32129; -.
DR BioGRID; 4261196; 13.
DR STRING; 511145.b3862; -.
DR PaxDb; P32129; -.
DR PRIDE; P32129; -.
DR EnsemblBacteria; AAC76860; AAC76860; b3862.
DR EnsemblBacteria; BAE77446; BAE77446; BAE77446.
DR GeneID; 948350; -.
DR KEGG; ecj:JW3834; -.
DR KEGG; eco:b3862; -.
DR PATRIC; fig|1411691.4.peg.2853; -.
DR EchoBASE; EB1780; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_054727_0_1_6; -.
DR InParanoid; P32129; -.
DR OMA; HHSWADI; -.
DR PhylomeDB; P32129; -.
DR BioCyc; EcoCyc:EG11833-MON; -.
DR BioCyc; MetaCyc:EG11833-MON; -.
DR PRO; PR:P32129; -.
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; IDA:EcoCyc.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Probable acyltransferase YihG"
FT /id="PRO_0000208206"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..35
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 103..108
FT /note="HXXXXD motif"
SQ SEQUENCE 310 AA; 36289 MW; 9F8E3F52EB0B186E CRC64;
MANLLNKFIM TRILAAITLL LSIVLTILVT IFCSVPIIIA GIVKLLLPVP VIWRKVSRFC
DFMMYCWCEG LAVLLHLNPH LQWEVHGLEG LSKKNWYLLI CNHRSWADIV VLCVLFRKHI
PMNKYFLKQQ LAWVPFLGLA CWSLDMPFMK RYSRAYLLRH PERRGKDVET TRRSCEKFRL
HPTTIVNFVE GSRFTQEKHQ QTHSTFQNLL PPKAAGIAMA LNVLGKQFDK LLNVTLCYPD
NNRQPFFDML SGKLTRIVVH VDLQPIADEL HGDYINDKSF KRHFQQWLNS LWQEKDRLLT
SLMSSQRQNK
