ID   ABLB_METMP              Reviewed;         274 AA.
AC   Q6LYX3;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Beta-lysine N(6)-acetyltransferase {ECO:0000305};
DE            EC=2.3.1.264 {ECO:0000269|PubMed:14532061};
GN   Name=ablB {ECO:0000303|PubMed:14532061}; Synonyms=yodP;
GN   OrderedLocusNames=MMP0862;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=14532061; DOI=10.1128/aem.69.10.6047-6055.2003;
RA   Pfluger K., Baumann S., Gottschalk G., Lin W., Santos H., Muller V.;
RT   "Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of
RT   methanogenic archaea are salt induced and are essential for the
RT   biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.";
RL   Appl. Environ. Microbiol. 69:6047-6055(2003).
CC   -!- FUNCTION: Catalyzes the acetylation of beta-lysine to N6-acetyl-beta-
CC       lysine, a compatible solute produced by methanogenic archaea that helps
CC       cells to cope with salt stress. {ECO:0000269|PubMed:14532061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3,6-diaminohexanoate + acetyl-CoA = (3S)-6-acetamido-3-
CC         aminohexanoate + CoA + H(+); Xref=Rhea:RHEA:33019, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57434,
CC         ChEBI:CHEBI:137165; EC=2.3.1.264;
CC         Evidence={ECO:0000269|PubMed:14532061};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking both ablA and ablB no longer
CC       produce N6-acetyl-beta-lysine and are incapable of growth at high salt
CC       concentrations. {ECO:0000269|PubMed:14532061}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR   EMBL; BX950229; CAF30418.1; -; Genomic_DNA.
DR   RefSeq; WP_011170806.1; NC_005791.1.
DR   AlphaFoldDB; Q6LYX3; -.
DR   STRING; 267377.MMP0862; -.
DR   EnsemblBacteria; CAF30418; CAF30418; MMP0862.
DR   GeneID; 2762074; -.
DR   KEGG; mmp:MMP0862; -.
DR   PATRIC; fig|267377.15.peg.887; -.
DR   eggNOG; arCOG04916; Archaea.
DR   HOGENOM; CLU_081246_0_0_2; -.
DR   OMA; LESMNVW; -.
DR   OrthoDB; 44864at2157; -.
DR   BioCyc; MetaCyc:MON-20162; -.
DR   BioCyc; MMAR267377:MMP_RS04485-MON; -.
DR   BRENDA; 2.3.1.264; 3262.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR022525; GNAT_AblB.
DR   InterPro; IPR000182; GNAT_dom.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR03827; GNAT_ablB; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..274
FT                   /note="Beta-lysine N(6)-acetyltransferase"
FT                   /id="PRO_0000423060"
FT   DOMAIN          123..274
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   274 AA;  31930 MW;  06F87D1A39D5EA19 CRC64;
     MEKIIEINDS IIQISDLNDR IYIMKLGKDV GELIKHVDSV CNEKKLSKVF AKVSGNKKEL
     FEKNGYICEG KLENYYSNDD AYFMSKFFEE SRKISKFSKE AEDVLNYVKT VGVNPHTKID
     EKFHLKIANE TDAEKLSKHY SKVFKTYPFP IDDPNYILKT MQTNVKYFII EDNGKIVAAS
     SCEMDIKNKC VEMTDFAVLE EYQKLGLSKY LLYIMEKIMK DNGYRVFYTI ARSISYGMNI
     TFKKMGYMYS GTAVNNTNIC GNFEDMNFWY KLSE