EIS_MYCBO
ID EIS_MYCBO Reviewed; 402 AA.
AC P59772; A0A1R3Y3C0; X2BKM2;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 97.
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};
GN OrderedLocusNames=BQ2027_MB2439C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP IDENTIFICATION.
RX PubMed=10629183; DOI=10.1128/jb.182.2.377-384.2000;
RA Wei J., Dahl J., Moulder J.W., Roberts E.A., O'Gaora P., Young D.B.,
RA Friedman R.L.;
RT "Identification of a Mycobacterium tuberculosis gene that enhances
RT mycobacterial survival in macrophages.";
RL J. Bacteriol. 182:377-384(2000).
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=SIU01054.1; 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; LT708304; SIU01054.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_856088.1; NC_002945.3.
DR AlphaFoldDB; P59772; -.
DR SMR; P59772; -.
DR EnsemblBacteria; SIU01054; SIU01054; BQ2027_MB2439C.
DR PATRIC; fig|233413.5.peg.2685; -.
DR Proteomes; UP000001419; Chromosome.
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_0000220261"
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; 43774 MW; 918549D65B01B372 CRC64;
MTVTLCSPTE DDWPGMFLLA AASFTDFIGP ESATAWRTLV PTDGAVVVRD GAGPGSEVVG
MALYMDLRLA 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
