ID S6BU46_9GAMM Unreviewed; 165 AA.
AC S6BU46;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:BAN69619.1};
GN ORFNames=EBS_1744 {ECO:0000313|EMBL:BAN69619.1};
OS endosymbiont of unidentified scaly snail isolate Monju.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN69619.1, ECO:0000313|Proteomes:UP000015562};
RN [1] {ECO:0000313|EMBL:BAN69619.1, ECO:0000313|Proteomes:UP000015562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Monju {ECO:0000313|EMBL:BAN69619.1};
RX PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT "Allying with armored snails: the complete genome of gammaproteobacterial
RT endosymbiont.";
RL ISME J. 8:40-51(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02210}.
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DR EMBL; AP012978; BAN69619.1; -; Genomic_DNA.
DR RefSeq; WP_043108354.1; NZ_AP012978.1.
DR AlphaFoldDB; S6BU46; -.
DR STRING; 1248727.EBS_1744; -.
DR KEGG; enm:EBS_1744; -.
DR HOGENOM; CLU_013985_23_2_6; -.
DR OrthoDB; 9796919at2; -.
DR Proteomes; UP000015562; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:UniProtKB-UniRule.
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; PTHR43617:SF20; [RIBOSOMAL PROTEIN S18]-ALANINE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43617; L-AMINO ACID N-ACETYLTRANSFERASE; 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 ECO:0000313|EMBL:BAN69619.1}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02210};
KW Reference proteome {ECO:0000313|Proteomes:UP000015562};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02210, ECO:0000313|EMBL:BAN69619.1}.
FT DOMAIN 10..156
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT ACT_SITE 111
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
FT BINDING 116
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02210"
SQ SEQUENCE 165 AA; 18412 MW; 62C3E15E855CF56F CRC64;
MSAVIQELQP TLRAMREGDL GAVFVNERAA YSHPWSMGIL RDCLRVGYHC MVAEFAGELA
GHAVLSTGAG EAHLLNLCVA PDWQGRGLGR RLLRRMLRIA REKDADTVYL EVRASNHVAR
ALYESEGFCE IGRRKGYYPH ERHEREDAVV YAKPMLTGSG AGFPR
//
