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
//