ID A0A060UZY5_9PROT Unreviewed; 156 AA.
AC A0A060UZY5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=[Ribosomal protein bS18]-alanine N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_02210};
DE EC=2.3.1.266 {ECO:0000256|HAMAP-Rule:MF_02210};
GN Name=rimI {ECO:0000256|HAMAP-Rule:MF_02210};
GN ORFNames=AFERRI_600200 {ECO:0000313|EMBL:CDQ11974.1};
OS Acidithiobacillus ferrivorans.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ11974.1, ECO:0000313|Proteomes:UP000029069};
RN [1] {ECO:0000313|EMBL:CDQ11974.1, ECO:0000313|Proteomes:UP000029069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ11974.1,
RC ECO:0000313|Proteomes:UP000029069};
RA Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V.,
RA Bonnefoy V.;
RT "Initial genome analysis of the psychrotolerant acidophile
RT Acidithiobacillus ferrivorans CF27: insights into iron and sulfur oxidation
RT pathways and into biofilm formation.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acetylates the N-terminal alanine of ribosomal protein bS18.
CC {ECO:0000256|HAMAP-Rule:MF_02210}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimI subfamily.
CC {ECO:0000256|ARBA:ARBA00005395, 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:CDQ11974.1}.
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DR EMBL; CCCS020000057; CDQ11974.1; -; Genomic_DNA.
DR RefSeq; WP_035195243.1; NZ_LT841305.1.
DR AlphaFoldDB; A0A060UZY5; -.
DR Proteomes; UP000029069; 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; PTHR43877; -; 1.
DR PANTHER; PTHR43877:SF2; AMINOALKYLPHOSPHONATE N-ACETYLTRANSFERASE-RELATED; 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|HAMAP-Rule:MF_02210};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:CDQ11974.1}.
FT DOMAIN 1..147
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 69..71
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 77..82
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 108
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 156 AA; 17262 MW; 4B159913E00F7D02 CRC64;
MNLRPMRAGD LDAVATLESH ISPGPWTRSI FRDCMQAGYD AWIMEDDAGV LVAFGVLSTG
AAEAHILNLG VAPTLRRRGF GRHMLQHLLC RAGQLGAQRA FLEVRVSNIG AQDLYRSQGF
HEIGVRLDYY RNEEGREDAL VLSLSLLPSV NQLREG
//
