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Database: UniProt/TrEMBL
Entry: C5D4E1_GEOSW
LinkDB: C5D4E1_GEOSW
Original site: C5D4E1_GEOSW 
ID   C5D4E1_GEOSW            Unreviewed;       150 AA.
AC   C5D4E1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=Ribosomal-protein-alanine acetyltransferase {ECO:0000256|RuleBase:RU363094};
DE            EC=2.3.1.128 {ECO:0000256|RuleBase:RU363094};
GN   OrderedLocusNames=GWCH70_0218 {ECO:0000313|EMBL:ACS23149.1};
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS23149.1, ECO:0000313|Proteomes:UP000002386};
RN   [1] {ECO:0000313|EMBL:ACS23149.1, ECO:0000313|Proteomes:UP000002386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70 {ECO:0000313|EMBL:ACS23149.1,
RC   ECO:0000313|Proteomes:UP000002386};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme acetylates the N-terminal alanine of
CC       ribosomal protein S18. {ECO:0000256|RuleBase:RU363094}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + ribosomal-protein L-alanine = CoA
CC       + ribosomal-protein N-acetyl-L-alanine.
CC       {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; CP001638; ACS23149.1; -; Genomic_DNA.
DR   RefSeq; WP_012748970.1; NC_012793.1.
DR   ProteinModelPortal; C5D4E1; -.
DR   STRING; 471223.GWCH70_0218; -.
DR   EnsemblBacteria; ACS23149; ACS23149; GWCH70_0218.
DR   KEGG; gwc:GWCH70_0218; -.
DR   eggNOG; ENOG410801F; Bacteria.
DR   eggNOG; COG0456; LUCA.
DR   HOGENOM; HOG000078523; -.
DR   KO; K03789; -.
DR   OMA; GERYLNY; -.
DR   OrthoDB; POG091H02FM; -.
DR   BioCyc; GSP471223:GH2C-265-MONOMER; -.
DR   Proteomes; UP000002386; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008999; F:ribosomal-protein-alanine N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002386};
KW   Cytoplasm {ECO:0000256|RuleBase:RU363094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002386};
KW   Transferase {ECO:0000313|EMBL:ACS23149.1}.
FT   DOMAIN        5    150       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   150 AA;  17329 MW;  0F520BC5C423E41F CRC64;
     MGMKIRFRSM TLNDIDAVLQ VEHASFTSPW SREAFYNELV YNRYAKYIVM EHNGRIIGYA
     GMWVVIDEAH ITNVAVLPEY RGKKLGEALM RKLMETAKQL GAVTMTLEVR VSNHVAQSLY
     RKLGFLNGGI RRHYYPDNLE DALVMWVKLS
//
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