ID A0A0A0C1D3_9CELL Unreviewed; 414 AA.
AC A0A0A0C1D3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:KGM13727.1};
GN ORFNames=N869_15830 {ECO:0000313|EMBL:KGM13727.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM13727.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM13727.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM13727.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM13727.1}.
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DR EMBL; AXCZ01000027; KGM13727.1; -; Genomic_DNA.
DR RefSeq; WP_035058470.1; NZ_AXCZ01000027.1.
DR AlphaFoldDB; A0A0A0C1D3; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000054314; 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:UP000054314};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 186..306
FT /note="Eis-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF17668"
FT DOMAIN 310..410
FT /note="Enhanced intracellular survival protein"
FT /evidence="ECO:0000259|Pfam:PF13530"
SQ SEQUENCE 414 AA; 44147 MW; BBAAF378B213B79D CRC64;
MTTPTPGYRT VTVDEARKAD LLTIDRWAFP SGLPDGAFAA LPVPLSWDRT RGVRSGSGDL
VAVHSSYPFQ GLPVPGGTVD AAGLTWVGVH PGHRRRGILR TMITDHLERT SARGEAVSVL
TASEPSIYGR FGYGSACPAL RLTVPRGAAL RDVPGAQDVH LEIETLDVAR HAPTIRALHG
RVGRPGWATR TTTALEASFL HDSEHTRDGH EPLRVVTASL DGTPTGYALF RRRLRWEDTA
ASGTVSVVEA VARDAATARA LWGALLDMDL MSGTEVGLLP VDDVLTHLLV DLRAAAPRLK
DHVWVRLVDL PAALRARRYA APVHVVLEVA DAMVPANAGR WRLQGGPDHA EVTRTDADPD
LVLDVRELGT VYLGGVSTAA LHAAGLVREV TAGAVARAAV AFGWPTAPGC SWVF
//
