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RSSA_SHIFL
ID   RSSA_SHIFL              Reviewed;         301 AA.
AC   P0AFR1; P37053; P37054;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=NTE family protein RssA;
GN   Name=rssA; OrderedLocusNames=SF1234, S1320;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
RC   STRAIN=Serotype 2a;
RX   PubMed=1406252; DOI=10.1111/j.1365-2958.1992.tb01385.x;
RA   Hromockyj A.E., Tucker S.C., Maurelli A.T.;
RT   "Temperature regulation of Shigella virulence: identification of the
RT   repressor gene virR, an analogue of hns, and partial complementation by
RT   tyrosyl transfer RNA (tRNA1(Tyr)).";
RL   Mol. Microbiol. 6:2113-2124(1992).
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=X66849; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN42847.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16732.1; -; Genomic_DNA.
DR   EMBL; X66849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_707140.2; NC_004337.2.
DR   RefSeq; WP_001295622.1; NZ_WPGW01000029.1.
DR   AlphaFoldDB; P0AFR1; -.
DR   SMR; P0AFR1; -.
DR   STRING; 198214.SF1234; -.
DR   PRIDE; P0AFR1; -.
DR   EnsemblBacteria; AAN42847; AAN42847; SF1234.
DR   EnsemblBacteria; AAP16732; AAP16732; S1320.
DR   GeneID; 1026307; -.
DR   GeneID; 58390553; -.
DR   KEGG; sfl:SF1234; -.
DR   KEGG; sfx:S1320; -.
DR   PATRIC; fig|198214.7.peg.1452; -.
DR   HOGENOM; CLU_047251_2_0_6; -.
DR   OMA; CSMPGLL; -.
DR   OrthoDB; 373926at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome.
FT   CHAIN           1..301
FT                   /note="NTE family protein RssA"
FT                   /id="PRO_0000172532"
FT   DOMAIN          8..168
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           39..43
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           155..157
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        41
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   CONFLICT        7
FT                   /note="G -> A (in Ref. 3; X66849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="G -> C (in Ref. 3; X66849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..70
FT                   /note="DV -> EL (in Ref. 3; X66849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="A -> P (in Ref. 3; X66849)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  33067 MW;  7AA66196B90A0C26 CRC64;
     MRKIKIGLAL GSGAARGWSH IGVINALKKV GIEIDIVAGC SIGSLVGAAY ACDRLSALED
     WVTSFSYWDV LRLMDLSWQR GGLLRGERVF NQYREIMPET EIENCSRRFA AVATNLSTGR
     ELWFTEGDLH LAIRASCSIP GLMAPVAHNG YWLVDGAVVN PIPISLTRAL GADIVIAVDL
     QHDAHLMQQD LLSFNVSEEN SENGDSLPWH ARLKERLGSI TTRRAVTAPT ATEIMTTSIQ
     VLENRLKRNR MAGDPPDILI QPVCPQISTL DFHRAHAAIA AGQLAVERKM DELLPLVRTN
     I
 
 
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