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Database: UniProt
Entry: A0A0T0MK80_9CELL
LinkDB: A0A0T0MK80_9CELL
Original site: A0A0T0MK80_9CELL 
ID   A0A0T0MK80_9CELL        Unreviewed;       422 AA.
AC   A0A0T0MK80;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:KQT01082.1};
GN   ORFNames=ASG23_05615 {ECO:0000313|EMBL:KQT01082.1};
OS   Cellulomonas sp. Leaf395.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1736362 {ECO:0000313|EMBL:KQT01082.1, ECO:0000313|Proteomes:UP000051971};
RN   [1] {ECO:0000313|EMBL:KQT01082.1, ECO:0000313|Proteomes:UP000051971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf395 {ECO:0000313|EMBL:KQT01082.1,
RC   ECO:0000313|Proteomes:UP000051971};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT01082.1, ECO:0000313|Proteomes:UP000051971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf395 {ECO:0000313|EMBL:KQT01082.1,
RC   ECO:0000313|Proteomes:UP000051971};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_01812}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC       {ECO:0000256|HAMAP-Rule:MF_01812}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT01082.1}.
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DR   EMBL; LMQI01000002; KQT01082.1; -; Genomic_DNA.
DR   RefSeq; WP_056021458.1; NZ_LMQI01000002.1.
DR   AlphaFoldDB; A0A0T0MK80; -.
DR   STRING; 1736362.ASG23_05615; -.
DR   OrthoDB; 8399956at2; -.
DR   Proteomes; UP000051971; Unassembled WGS sequence.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.630.30; -; 2.
DR   Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 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; IPR022902; NAcTrfase_Eis.
DR   InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR   PANTHER; PTHR37817; N-ACETYLTRANSFERASE EIS; 1.
DR   PANTHER; PTHR37817:SF1; N-ACETYLTRANSFERASE EIS; 1.
DR   Pfam; PF17668; Acetyltransf_17; 1.
DR   Pfam; PF13527; Acetyltransf_9; 1.
DR   Pfam; PF13530; SCP2_2; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF55718; SCP-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01812}; Reference proteome {ECO:0000313|Proteomes:UP000051971};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01812}.
FT   DOMAIN          187..299
FT                   /note="Eis-like acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF17668"
FT   DOMAIN          315..418
FT                   /note="Enhanced intracellular survival protein"
FT                   /evidence="ECO:0000259|Pfam:PF13530"
SQ   SEQUENCE   422 AA;  45707 MW;  9F978DE67DB2A041 CRC64;
     MSPLPDGYRH VDVPESRTTE FLEVDRLAFA FDSNAETDAL VPITFEWDRA QAVEDQDGRL
     VSVHASYAHA MPVPGATIAC SGLTWVGTRP DQRRRGLLRA AIDSHFARSL ARDEPISALF
     AAEHSIYGRF GYGSAADHVR VKLPRGAALR DVPGADELEV RLATVDVARD SAVVDTVHRA
     AGAGRPGWTT RDSDAWRTRV LVDPPAWREG AEPLRIVTVH DAAGQVRAYA LFRRKENWAD
     GGAAGTVLVR EAVAVDAAAT HRLWSFLLDL DLTATVEGPM LPVDDALLHL LLDPRAVVPK
     VNDNLWVRLL DLPVALVGRR YSAPVDAVLD VTDTHLTANA GRWRLTTGER QDDGTYAAQV
     TPTQDDADLT LDVRELGAVY LGGRSLAALA RAGLVSEATP GALQSAAVAF LWPVAPMCTY
     VW
//
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