ID   EIS_MYCBT               Reviewed;         402 AA.
AC   C1AQY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=N-acetyltransferase Eis {ECO:0000255|HAMAP-Rule:MF_01812};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
DE   AltName: Full=Enhanced intracellular survival protein {ECO:0000255|HAMAP-Rule:MF_01812};
DE   AltName: Full=Protein-lysine N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01812};
GN   Name=eis {ECO:0000255|HAMAP-Rule:MF_01812}; OrderedLocusNames=JTY_2426;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
CC   -!- FUNCTION: Effector that is released into the host cell and affects host
CC       immune responses. Acts as an acetyltransferase that acetylates lysine
CC       residues of host proteins. {ECO:0000255|HAMAP-Rule:MF_01812}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01812};
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01812}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_01812}. Host
CC       cytoplasmic vesicle, host phagosome {ECO:0000255|HAMAP-Rule:MF_01812}.
CC       Extracellular vesicle, bacterial extracellular vesicle
CC       {ECO:0000255|HAMAP-Rule:MF_01812}. Host extracellular space
CC       {ECO:0000255|HAMAP-Rule:MF_01812}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC       {ECO:0000255|HAMAP-Rule:MF_01812}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH26710.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AP010918; BAH26710.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C1AQY1; -.
DR   SMR; C1AQY1; -.
DR   KEGG; mbt:JTY_2426; -.
DR   HOGENOM; CLU_050659_0_0_11; -.
DR   GO; GO:0097691; C:bacterial extracellular vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043655; C:host extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1050.10; -; 1.
DR   HAMAP; MF_01812; Eis; 1.
DR   InterPro; IPR041380; Acetyltransf_17.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR025559; Eis_dom.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR022902; NAcTrfase_Eis.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   Pfam; PF17668; Acetyltransf_17; 1.
DR   Pfam; PF13530; SCP2_2; 1.
DR   SUPFAM; SSF55718; SSF55718; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Host cytoplasmic vesicle; Secreted; Transferase.
FT   CHAIN           1..402
FT                   /note="N-acetyltransferase Eis"
FT                   /id="PRO_1000187720"
FT   DOMAIN          3..154
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   ACT_SITE        126
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   ACT_SITE        402
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   BINDING         85..87
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   BINDING         93..98
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   BINDING         121..122
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ   SEQUENCE   402 AA;  43804 MW;  EF06F75C00F05333 CRC64;
     MTVTLCSPTE DDWPGMFLLA AASFTDFIGP ESATAWRTLV PTDGAVVVRD GAGPGSEVVG
     MALYMDLRLT VPGEVVLPTA GLSFVAVAPT HRRRGLLRAM CAELHRRIAD SGYPVAALHA
     SEGGIYGRFG YGPATTLHEL TVDRRFARFH ADAPGGGLGG SSVRLVRPTE HRGEFEAIYE
     RWRQQVPGGL LRPQVLWDEL LAECKAAPGG DRESFALLHP DGYALYRVDR TDLKLARVSE
     LRAVTADAHC ALWRALIGLD SMERISIITH PQDPLPHLLT DTRLARTTWR QDGLWLRIMN
     VPAALEARGY AHEVGEFSTV LEVSDGGRFA LKIGDGRARC TPTDAAAEIE MDRDVLGSLY
     LGAHRASTLA AANRLRTKDS QLLRRLDAAF ASDVPVQTAF EF