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YJAB_SALTY
ID   YJAB_SALTY              Reviewed;         145 AA.
AC   P40677;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Peptidyl-lysine N-acetyltransferase YjaB {ECO:0000250|UniProtKB:P09163};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P09163};
DE   AltName: Full=KAT {ECO:0000250|UniProtKB:P09163};
GN   Name=yjaB; OrderedLocusNames=STM4181;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
RX   PubMed=1729233; DOI=10.1128/jb.174.2.390-397.1992;
RA   Mares R., Urbanowski M.L., Stauffer G.V.;
RT   "Regulation of the Salmonella typhimurium metA gene by the metR protein and
RT   homocysteine.";
RL   J. Bacteriol. 174:390-397(1992).
CC   -!- FUNCTION: N-epsilon-lysine acetyltransferase that catalyzes acetylation
CC       of a large number of proteins. {ECO:0000250|UniProtKB:P09163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000250|UniProtKB:P09163};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL23005.1; -; Genomic_DNA.
DR   EMBL; M74188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_463046.1; NC_003197.2.
DR   RefSeq; WP_000973243.1; NC_003197.2.
DR   AlphaFoldDB; P40677; -.
DR   SMR; P40677; -.
DR   STRING; 99287.STM4181; -.
DR   PaxDb; P40677; -.
DR   EnsemblBacteria; AAL23005; AAL23005; STM4181.
DR   GeneID; 1255707; -.
DR   KEGG; stm:STM4181; -.
DR   PATRIC; fig|99287.12.peg.4393; -.
DR   HOGENOM; CLU_013985_21_0_6; -.
DR   PhylomeDB; P40677; -.
DR   BioCyc; SENT99287:STM4181-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF13673; Acetyltransf_10; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..145
FT                   /note="Peptidyl-lysine N-acetyltransferase YjaB"
FT                   /id="PRO_0000074616"
FT   DOMAIN          3..144
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   CONFLICT        95..102
FT                   /note="ALTLAPGL -> GVNTGAGI (in Ref. 2; M74188)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   145 AA;  16344 MW;  CC7A8C84B5F1C397 CRC64;
     MMINIRRSRH EEGEKLIAIW RRSVDATHDF LSNAYRAELE ELVSDFLPEA PLWVAVTDQD
     EPVGFMLLTG EHMDALFIDP DVRGQGIGKM LVEHALTLAP GLTTNVNEQN TQAVGFYKKM
     GFKVTGRSEV DDLGKPYPLL NLIYP
 
 
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