ID A0A0Q5JUD9_9MICO Unreviewed; 434 AA.
AC A0A0Q5JUD9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQR21129.1};
GN ORFNames=ASF76_12645 {ECO:0000313|EMBL:KQR21129.1};
OS Microbacterium sp. Leaf151.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR21129.1, ECO:0000313|Proteomes:UP000051582};
RN [1] {ECO:0000313|EMBL:KQR21129.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR21129.1,
RC ECO:0000313|Proteomes:UP000051582};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR21129.1, ECO:0000313|Proteomes:UP000051582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf151 {ECO:0000313|EMBL:KQR21129.1,
RC ECO:0000313|Proteomes:UP000051582};
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:KQR21129.1}.
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DR EMBL; LMOR01000004; KQR21129.1; -; Genomic_DNA.
DR RefSeq; WP_055958316.1; NZ_LMOR01000004.1.
DR AlphaFoldDB; A0A0Q5JUD9; -.
DR STRING; 1736276.ASF76_12645; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000051582; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 217..326
FT /note="Eis-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF17668"
FT DOMAIN 329..428
FT /note="Enhanced intracellular survival protein"
FT /evidence="ECO:0000259|Pfam:PF13530"
SQ SEQUENCE 434 AA; 46511 MW; 58DFB783C8BEEE03 CRC64;
MASIDPLTLP LDQTSAADLA ASGLDYARVD ADGDAYRPFQ RAVARGFLGG ESTDDEAENA
RLTLRTRRLT AVYDRDGVEP GVPVGTVDSW ATELTTSPGR QTDLWAISAV TVAPTHRRRG
IARAMLGGEL RTAAAAGFAL AGLTVTEATI YGRWGFSPAT WASDVEVDTT RARWTGPTPT
GRLDFVPRDG LADRVSAVHE RVRRQRPGSV PGWDGRWRGI AGVAPGDKEG EKVRAVAYRD
TDGVERGIVV YTIADRDDFA AHDLSVRALF AESPDAYAAL WRFVLEHDLV GTVKAWLQAP
VPPVQWMVTD RRAVTATLTD HQWLRVLDVP HALASRAYAA PLRVAVRVTD PLGFADGAWR
LVIGDDGEAV VEPVSDGDSV DVEMTVNALG SILLGGARAT ELAAAGIVSG HTGVLAAIDR
SFAPSMTPLL DIWY
//
