YWNH_BACSU
ID YWNH_BACSU Reviewed; 163 AA.
AC P71043; Q795A0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative phosphinothricin acetyltransferase YwnH;
DE Short=PPT N-acetyltransferase;
DE EC=2.3.1.183;
GN Name=ywnH; OrderedLocusNames=BSU36560;
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=9150240; DOI=10.1128/jb.179.10.3371-3373.1997;
RA Cruz-Ramos H., Glaser P., Wray L.V. Jr., Fisher S.H.;
RT "The Bacillus subtilis ureABC operon.";
RL J. Bacteriol. 179:3371-3373(1997).
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 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: This enzyme is an effector of phosphinothricin tripeptide
CC (PTT or bialaphos) resistance. Inactivates PTT by transfer of an acetyl
CC group (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + phosphinothricin = CoA + H(+) + N-
CC acetylphosphinothricin; Xref=Rhea:RHEA:12597, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58879,
CC ChEBI:CHEBI:58882; EC=2.3.1.183;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.
CC {ECO:0000305}.
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DR EMBL; Y08559; CAA69854.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15673.1; -; Genomic_DNA.
DR PIR; B70064; B70064.
DR RefSeq; NP_391537.1; NC_000964.3.
DR RefSeq; WP_010886629.1; NZ_JNCM01000034.1.
DR PDB; 1VHS; X-ray; 1.80 A; A/B=2-163.
DR PDBsum; 1VHS; -.
DR AlphaFoldDB; P71043; -.
DR SMR; P71043; -.
DR STRING; 224308.BSU36560; -.
DR jPOST; P71043; -.
DR PaxDb; P71043; -.
DR EnsemblBacteria; CAB15673; CAB15673; BSU_36560.
DR GeneID; 936956; -.
DR KEGG; bsu:BSU36560; -.
DR PATRIC; fig|224308.43.peg.3830; -.
DR eggNOG; COG1247; Bacteria.
DR InParanoid; P71043; -.
DR OMA; IFAHNQP; -.
DR PhylomeDB; P71043; -.
DR BioCyc; BSUB:BSU36560-MON; -.
DR EvolutionaryTrace; P71043; -.
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:0102971; F:phosphinothricin N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0009635; P:response to herbicide; 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 3D-structure; Acyltransferase; Antibiotic resistance; Herbicide resistance;
KW Reference proteome; Transferase.
FT CHAIN 1..163
FT /note="Putative phosphinothricin acetyltransferase YwnH"
FT /id="PRO_0000360167"
FT DOMAIN 1..158
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 85..87
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255"
FT BINDING 94..98
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255"
FT BINDING 124..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:1VHS"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1VHS"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 137..148
FT /evidence="ECO:0007829|PDB:1VHS"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:1VHS"
SQ SEQUENCE 163 AA; 18364 MW; 8A7F397CE61B8265 CRC64;
MTLRLAEHRD LEAVVAIYNS TIASRMVTAD TEPVTPEDRM EWFSGHTESR PLYVAEDENG
NVAAWISFET FYGRPAYNKT AEVSIYIDEA CRGKGVGSYL LQEALRIAPN LGIRSLMAFI
FGHNKPSLKL FEKHGFAEWG LFPGIAEMDG KRYDLKILGR ELS
