ID Q6MK55_BDEBA Unreviewed; 188 AA.
AC Q6MK55;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=[ribosomal protein S5]-alanine N-acetyltransferase {ECO:0000256|ARBA:ARBA00039124};
DE EC=2.3.1.267 {ECO:0000256|ARBA:ARBA00039124};
GN OrderedLocusNames=Bd2558 {ECO:0000313|EMBL:CAE80354.1};
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE80354.1, ECO:0000313|Proteomes:UP000008080};
RN [1] {ECO:0000313|EMBL:CAE80354.1, ECO:0000313|Proteomes:UP000008080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC {ECO:0000313|Proteomes:UP000008080};
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[ribosomal protein uS5] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein uS5];
CC Xref=Rhea:RHEA:43752, Rhea:RHEA-COMP:10672, Rhea:RHEA-COMP:10673,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.267;
CC Evidence={ECO:0000256|ARBA:ARBA00036822};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. RimJ subfamily.
CC {ECO:0000256|ARBA:ARBA00038502}.
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DR EMBL; BX842653; CAE80354.1; -; Genomic_DNA.
DR RefSeq; WP_011164957.1; NC_005363.1.
DR AlphaFoldDB; Q6MK55; -.
DR STRING; 264462.Bd2558; -.
DR KEGG; bba:Bd2558; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_013985_40_1_7; -.
DR Proteomes; UP000008080; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008999; F:peptide-alanine-alpha-N-acetyltransferase activity; IEA:RHEA.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR43792:SF8; [RIBOSOMAL PROTEIN S5]-ALANINE N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR43792; GNAT FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00765)-RELATED-RELATED; 1.
DR Pfam; PF13302; Acetyltransf_3; 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,
KW ECO:0000313|EMBL:CAE80354.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAE80354.1}.
FT DOMAIN 15..177
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 188 AA; 22084 MW; 5632D1AE14218C2D CRC64;
MKSIDLPIVK KTARLILRPL EATDYENWVQ AYSSMRPPQN EWDETNWAES ELTPKKFKEL
LKSEKDQRHR DHFYSFGVFL KDDGTLIGQV SLMDISRAVF QNAYVGYRIF NNYWGYGFAQ
EATRGCIDIA FKKLKLHRVE AGIAPTNKRS IKVAKALKMR KEGLSKRRLL VHKKWQDMEI
WALTKEEL
//
