ID A0A143QA49_9NOCA Unreviewed; 404 AA.
AC A0A143QA49;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Enhanced intracellular survival protein {ECO:0000313|EMBL:AMY20105.1};
GN Name=eis_2 {ECO:0000313|EMBL:AMY20105.1};
GN ORFNames=A3Q40_02738 {ECO:0000313|EMBL:AMY20105.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY20105.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY20105.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY20105.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-2016) 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|ARBA:ARBA00009213, ECO:0000256|HAMAP-Rule:MF_01812}.
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DR EMBL; CP015219; AMY20105.1; -; Genomic_DNA.
DR RefSeq; WP_068102895.1; NZ_CP015219.1.
DR AlphaFoldDB; A0A143QA49; -.
DR STRING; 1653478.A3Q40_02738; -.
DR KEGG; rhu:A3Q40_02738; -.
DR PATRIC; fig|1653478.3.peg.2772; -.
DR Proteomes; UP000076180; Chromosome.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
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; IPR000182; GNAT_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.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01812}; Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 7..156
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 404 AA; 44886 MW; 3079869AE11175F0 CRC64;
MTTDDTITLR LATEDDWDAI ALLDAHAFGE HQNSEDMAET KLLTASSEIF LACDGDLPVG
VTMHFPMDVT VPGGTTLPAT GVSWVSVAPT HRRRGILRRM FTAQHERFEE AGKPLSVLTA
SEATIYERFG YGPATQGVTY SIDRRFAAFR PDLPPPVGAR LVTSEQAREL LPDIHRRWQQ
RTPGAQPMPQ TRWQRFFADR KNARGGFSKL FFVVHPDGYV AFRRGYRVGT AGAQDARIVD
FRAVTDEARS ALWQVLCGID LVETFEVTLP VGDPLLTLLT DRRVPQVQSV KDGLWVRLMD
VPAALSARTY AVDTDLTVAV EDPFLNAGGV FRMVVRDGHA DVVRTDREPD ITVSSSVLGS
LYLGAHRARQ FAAANRVQAT SERALHEFDL TFGTPRQPEI GWFF
//
