ID YVBK_BACSU Reviewed; 155 AA.
AC O32248;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Uncharacterized N-acetyltransferase YvbK;
DE EC=2.3.1.-;
GN Name=yvbK; OrderedLocusNames=BSU33890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RC STRAIN=168;
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the Bacillis subtilis acetyltransferase in complex
RT with CoA, northeast structural genomics target SR237.";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- FUNCTION: Probable N-acetyltransferase.
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DR EMBL; AL009126; CAB15394.1; -; Genomic_DNA.
DR PIR; B70030; B70030.
DR RefSeq; NP_391269.1; NC_000964.3.
DR RefSeq; WP_003228335.1; NZ_JNCM01000033.1.
DR PDB; 1YVK; X-ray; 3.01 A; A/B/C/D=1-155.
DR PDBsum; 1YVK; -.
DR AlphaFoldDB; O32248; -.
DR SMR; O32248; -.
DR STRING; 224308.BSU33890; -.
DR DrugBank; DB01992; Coenzyme A.
DR jPOST; O32248; -.
DR PaxDb; 224308-BSU33890; -.
DR EnsemblBacteria; CAB15394; CAB15394; BSU_33890.
DR GeneID; 938642; -.
DR KEGG; bsu:BSU33890; -.
DR PATRIC; fig|224308.43.peg.3552; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; O32248; -.
DR OrthoDB; 162775at2; -.
DR PhylomeDB; O32248; -.
DR BioCyc; BSUB:BSU33890-MONOMER; -.
DR EvolutionaryTrace; O32248; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR13947; GNAT FAMILY N-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR13947:SF37; N-ACETYLTRANSFERASE 14-RELATED; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..155
FT /note="Uncharacterized N-acetyltransferase YvbK"
FT /id="PRO_0000359974"
FT DOMAIN 6..155
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 69..71
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 77..82
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 111..117
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1YVK"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1YVK"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1YVK"
SQ SEQUENCE 155 AA; 17745 MW; 45966AB5F18D1443 CRC64;
MNMQKLRIEL GEETNDELYD LLLLADPSKD IVDEYLERGE CYTAWAGDEL AGVYVLLKTR
PQTVEIVNIA VKESLQKKGF GKQLVLDAIE KAKKLGADTI EIGTGNSSIH QLSLYQKCGF
RIQAIDHDFF LRHYDEDIFE NGIQCRDMVR LYLDL
//
