ID   ABLB_METMA              Reviewed;         271 AA.
AC   Q8PYC8;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 113.
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}; OrderedLocusNames=MM_0935;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN   [2]
RP   IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, GENE NAME, INDUCTION, AND
RP   OPERON STRUCTURE.
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
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:0000305|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   -!- INDUCTION: Transcription is induced at high salt concentrations. Forms
CC       part of an operon with ablA. {ECO:0000269|PubMed:14532061}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008384; AAM30631.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8PYC8; -.
DR   SMR; Q8PYC8; -.
DR   STRING; 192952.MM_0935; -.
DR   EnsemblBacteria; AAM30631; AAM30631; MM_0935.
DR   KEGG; mma:MM_0935; -.
DR   PATRIC; fig|192952.21.peg.1102; -.
DR   eggNOG; arCOG04916; Archaea.
DR   HOGENOM; CLU_081246_0_0_2; -.
DR   OMA; LESMNVW; -.
DR   BRENDA; 2.3.1.264; 3270.
DR   Proteomes; UP000000595; 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..271
FT                   /note="Beta-lysine N(6)-acetyltransferase"
FT                   /id="PRO_0000423059"
FT   DOMAIN          121..269
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          86..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..111
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  31027 MW;  6CBA275E5CC80AB9 CRC64;
     MDFIGRFEEI AGALKALAGT EKMGKIIVYT PPEKKDEPET CGYMEEGIIR RYYAGKDCHI
     YSNYPESSRE ISFHKEKEDR IIKNCLRKDR GTGKNQKKKK ISRKKDNWKK RKEKSRLPEG
     YTLRPAVQAD ASAMASLYSQ GFELYPTPLH MENYILETMH SNVLYFLVEK YGKIVSLASA
     EMDPKNRNAE ITDCLTIPSE RGKGHMKELI RALEKELSER SFLISYTLCR ASAPGINAAF
     SSLGYAFTGR LVNNCRIGNG FEDMNIWCRM L