STA_BACSU
ID STA_BACSU Reviewed; 173 AA.
AC P37506;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Streptothricin acetyltransferase A {ECO:0000303|PubMed:28842538};
DE EC=2.3.-.- {ECO:0000269|PubMed:28842538};
GN Name=satA {ECO:0000303|PubMed:28842538}; Synonyms=yyaR;
GN OrderedLocusNames=BSU40740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=28842538; DOI=10.1128/aem.01590-17;
RA Burckhardt R.M., Escalante-Semerena J.C.;
RT "In Bacillus subtilis, the SatA (formerly YyaR) acetyltransferase
RT detoxifies streptothricin via lysine acetylation.";
RL Appl. Environ. Microbiol. 83:E01590-E01590(2017).
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:28842538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + streptothricin D = CoA + H(+) + N(beta)-
CC acetylstreptothricin D; Xref=Rhea:RHEA:57004, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:60829,
CC ChEBI:CHEBI:141396; Evidence={ECO:0000269|PubMed:28842538};
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:28842538};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for streptothricin {ECO:0000269|PubMed:28842538};
CC KM=107 uM for acetyl-CoA {ECO:0000269|PubMed:28842538};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28842538}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is susceptible to streptothricin.
CC {ECO:0000269|PubMed:28842538}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
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DR EMBL; D26185; BAA05205.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16111.1; -; Genomic_DNA.
DR PIR; S65999; S65999.
DR RefSeq; NP_391954.1; NC_000964.3.
DR RefSeq; WP_003242546.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P37506; -.
DR SMR; P37506; -.
DR STRING; 224308.BSU40740; -.
DR PaxDb; P37506; -.
DR PRIDE; P37506; -.
DR EnsemblBacteria; CAB16111; CAB16111; BSU_40740.
DR GeneID; 937878; -.
DR KEGG; bsu:BSU40740; -.
DR PATRIC; fig|224308.179.peg.4416; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; P37506; -.
DR OMA; WNHYAYI; -.
DR PhylomeDB; P37506; -.
DR BioCyc; BSUB:BSU40740-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
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 InterPro; IPR008125; Streptothricin_AcTrfase.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR PRINTS; PR01754; SACTRNSFRASE.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Reference proteome; Transferase.
FT CHAIN 1..173
FT /note="Streptothricin acetyltransferase A"
FT /id="PRO_0000050058"
FT DOMAIN 21..173
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 173 AA; 20393 MW; 0FB09B59F6A056BE CRC64;
MIMKMTHLNM KDFNKPNEPF VVFGRMIPAF ENGVWTYTEE RFSKPYFKQY EDDDMDVSYV
EEEGKAAFLY YLENNCIGRI KIRSNWNGYA LIEDIAVAKD YRKKGVGTAL LHKAIEWAKE
NHFCGLMLET QDINISACHF YAKHHFIIGA VDTMLYSNFP TANEIAIFWY YKF
