(data stored in SCRATCH zone)

SWISSPROT: D6ZB84_SEGRD

ID   D6ZB84_SEGRD            Unreviewed;       154 AA.
AC   D6ZB84;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=[Ribosomal protein S18]-alanine N-acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE            EC=2.3.1.266 {ECO:0000256|RuleBase:RU363094};
GN   OrderedLocusNames=Srot_0356 {ECO:0000313|EMBL:ADG96843.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96843.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96843.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein
CC       S18. {ECO:0000256|RuleBase:RU363094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18]
CC         = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal
CC         protein bS18]; Xref=Rhea:RHEA:43756, Rhea:RHEA-COMP:10676,
CC         Rhea:RHEA-COMP:10677, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683;
CC         EC=2.3.1.266; Evidence={ECO:0000256|RuleBase:RU363094};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363094}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. RimI
CC       subfamily. {ECO:0000256|RuleBase:RU363094}.
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DR   EMBL; CP001958; ADG96843.1; -; Genomic_DNA.
DR   RefSeq; WP_013137299.1; NC_014168.1.
DR   STRING; 640132.Srot_0356; -.
DR   EnsemblBacteria; ADG96843; ADG96843; Srot_0356.
DR   KEGG; srt:Srot_0356; -.
DR   eggNOG; ENOG41080WA; Bacteria.
DR   eggNOG; COG0456; LUCA.
DR   HOGENOM; HOG000078523; -.
DR   KO; K03789; -.
DR   OMA; GERYLNY; -.
DR   OrthoDB; 1390922at2; -.
DR   BioCyc; SROT640132:G1GLH-357-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:UniProtKB-UniRule.
DR   InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01575; rimI; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZB84.
DR   SWISS-2DPAGE; D6ZB84.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000313|EMBL:ADG96843.1}.
FT   DOMAIN        5    149       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   154 AA;  16768 MW;  FAEEC9699809E3B7 CRC64;
     MTAWATVDAL REVDLPRVVE IDQLLFQQEG PWTLAMFQGD LKAAHTRYFA ARDLQGAVLG
     FAGVALLADA AEVITIGVDP VVQRTGAGRA LLGALLYEAE GRDVFLEVRV DNEPAIALYT
     AEGFEKVSVR KNYYRRVGKD AVVMRRPAEF GGGA
//

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