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Database: UniProt
Entry: K2JPJ8_9GAMM
LinkDB: K2JPJ8_9GAMM
Original site: K2JPJ8_9GAMM 
ID   K2JPJ8_9GAMM            Unreviewed;       144 AA.
AC   K2JPJ8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
DE            EC=2.3.1.266 {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
GN   Name=rimI {ECO:0000256|HAMAP-Rule:MF_02210};
GN   ORFNames=B3C1_11297 {ECO:0000313|EMBL:EKE72414.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE72414.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE72414.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE72414.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(2012).
CC   -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC       {ECO:0000256|HAMAP-Rule:MF_02210, 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 protein
CC         bS18]; Xref=Rhea:RHEA:43756, Rhea:RHEA-COMP:10676, Rhea:RHEA-
CC         COMP:10677, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.266;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02210,
CC         ECO:0000256|RuleBase:RU363094};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210,
CC       ECO:0000256|RuleBase:RU363094}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC       {ECO:0000256|ARBA:ARBA00005395, ECO:0000256|HAMAP-Rule:MF_02210,
CC       ECO:0000256|RuleBase:RU363094}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02210}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKE72414.1}.
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DR   EMBL; AMRI01000014; EKE72414.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2JPJ8; -.
DR   STRING; 745411.B3C1_11297; -.
DR   PATRIC; fig|745411.4.peg.2219; -.
DR   eggNOG; COG0456; Bacteria.
DR   Proteomes; UP000006755; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   HAMAP; MF_02210; RimI; 1.
DR   InterPro; IPR006464; AcTrfase_RimI/Ard1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR043690; RimI.
DR   NCBIfam; TIGR01575; rimI; 1.
DR   PANTHER; PTHR43420; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43420:SF51; PEPTIDYL-LYSINE N-ACETYLTRANSFERASE YIAC; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_02210};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000256|RuleBase:RU363094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006755};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02210}.
FT   DOMAIN          1..144
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   ACT_SITE        100
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT   BINDING         105
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ   SEQUENCE   144 AA;  15945 MW;  0DC300E3327E369B CRC64;
     MLSTASKADL SLLAHVEASQ HYPWTDNQLA SCFDSGYRVR LLWQDDEVVG FSICQRVLDE
     STLFNLCVLP QCRGLGYGKV LMADLIEDAK AASDSVIFLE VRASNQTAIG LYLKSGFSEV
     GRRKGYYRCH DGREDAVVMA LSLS
//
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