STA_STRLA
ID STA_STRLA Reviewed; 189 AA.
AC P08457;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Streptothricin acetyltransferase {ECO:0000303|PubMed:3015852, ECO:0000303|PubMed:3106324};
DE Short=STAT {ECO:0000303|PubMed:3106324};
DE EC=2.3.-.- {ECO:0000269|PubMed:3624064};
GN Name=sta {ECO:0000303|PubMed:3106324};
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3106324; DOI=10.1128/jb.169.5.1929-1937.1987;
RA Horinouchi S., Furuya K., Nishiyama M., Suzuki H., Beppu T.;
RT "Nucleotide sequence of the streptothricin acetyltransferase gene from
RT Streptomyces lavendulae and its expression in heterologous hosts.";
RL J. Bacteriol. 169:1929-1937(1987).
RN [2]
RP PRELIMINARY FUNCTION.
RX PubMed=3015852; DOI=10.7164/antibiotics.39.688;
RA Kobayashi T., Uozumi T., Beppu T.;
RT "Cloning and characterization of the streptothricin-resistance gene which
RT encodes streptothricin acetyltransferase from Streptomyces lavendulae.";
RL J. Antibiot. 39:688-693(1986).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3624064; DOI=10.7164/antibiotics.40.1016;
RA Kobayashi T., Horinouchi S., Uozumi T., Beppu T.;
RT "Purification and biochemical characterization of streptothricin
RT acetyltransferase coded by the cloned streptothricin-resistance gene of
RT Streptomyces lavendulae.";
RL J. Antibiot. 40:1016-1022(1987).
CC -!- FUNCTION: Involved in resistance to streptothricin, a broad-spectrum
CC antibiotic produced by streptomycetes. Detoxifies streptothricin via
CC acetylation of the beta amino group of the first beta-lysyl moiety of
CC streptothricin. {ECO:0000269|PubMed:3624064,
CC ECO:0000305|PubMed:3015852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + streptothricin F = CoA + H(+) + N(beta)-
CC acetylstreptothricin F; Xref=Rhea:RHEA:57000, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:60822,
CC ChEBI:CHEBI:141394; Evidence={ECO:0000269|PubMed:3624064};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for S-acetyl CoA {ECO:0000269|PubMed:3624064};
CC KM=2.3 uM for streptothricin F {ECO:0000269|PubMed:3624064};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:3624064};
CC Temperature dependence:
CC Stable at 35 degrees Celsius. Rapid inactivation occurs at 50 degrees
CC Celsius. {ECO:0000269|PubMed:3624064};
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
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DR EMBL; M16183; AAA88560.1; -; Genomic_DNA.
DR PIR; A26872; A26872.
DR RefSeq; WP_063854936.1; NG_048077.1.
DR AlphaFoldDB; P08457; -.
DR SMR; P08457; -.
DR BioCyc; MetaCyc:MON-15932; -.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Transferase.
FT CHAIN 1..189
FT /note="Streptothricin acetyltransferase"
FT /id="PRO_0000068587"
FT DOMAIN 44..189
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 55..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 189 AA; 20032 MW; 7BCA8AA2682654AC CRC64;
MTTTHGSTYE FRSARPGDAE AIEGLDGSFT TSTVFEVDVT GDGFALREVP ADPPLVKVFP
DDGGSDGEDG AEGEDADSRT FVAVGADGDL AGFAAVSYSA WNQRLTIEDI EVAPGHRGKG
IGRVLMRHAA DFARERGAGH LWLEVTNVNA PAIHAYRRMG FAFCGLDSAL YQGTASEGEH
ALYMSMPCP