YNGI_BACSU
ID YNGI_BACSU Reviewed; 549 AA.
AC O31826; O32301;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative acyl-CoA synthetase YngI;
DE EC=6.2.1.-;
GN Name=yngI; OrderedLocusNames=BSU18250;
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=9387222; DOI=10.1099/00221287-143-11-3443;
RA Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.;
RT "Sequence completion, identification and definition of the fengycin operon
RT in Bacillus subtilis 168.";
RL Microbiology 143:3443-3450(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).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74222.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y13917; CAA74222.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB13708.1; -; Genomic_DNA.
DR PIR; F69893; F69893.
DR RefSeq; NP_389707.1; NC_000964.3.
DR RefSeq; WP_003244755.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31826; -.
DR SMR; O31826; -.
DR STRING; 224308.BSU18250; -.
DR PaxDb; O31826; -.
DR PRIDE; O31826; -.
DR DNASU; 939571; -.
DR EnsemblBacteria; CAB13708; CAB13708; BSU_18250.
DR GeneID; 939571; -.
DR KEGG; bsu:BSU18250; -.
DR PATRIC; fig|224308.179.peg.1991; -.
DR eggNOG; COG0318; Bacteria.
DR InParanoid; O31826; -.
DR OMA; CEQYISV; -.
DR PhylomeDB; O31826; -.
DR BioCyc; BSUB:BSU18250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..549
FT /note="Putative acyl-CoA synthetase YngI"
FT /id="PRO_0000389244"
FT BINDING 198..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 549 AA; 61429 MW; 7CA52EF8C856FCE3 CRC64;
MAELIHSTIG RLLEQTADAY PDRDAVVYPD RNIRYTYAQF DSLCRQTAKG LMRMGIGKGD
HVAIWASNIS EWLAVQFATA KIGAVLVTVN TNYQAHELDY LLKQSDAAAL IIMDSYRGTS
YPDIVNSLIP ELQEAKPGQL KSERYPFLKT LIYIGNKRLS GMYHWDDTEI LAKTVTDAEL
EERMNSLDKD NVINMQYTSG TTGFPKGVML THFNVINNAA NIAECMALTS QDRMCIPVPF
FHCFGCVLGV LACVSVGAAM IPVQEFDPVT VLKTVEKEKC TVLHGVPTMF IAELHHPDFD
AYDLSTLRTG IMAGSPCPSE VMKAVIERMG MKDITIAYGQ TEASPVITQT RANDSFIRRV
ETTGRALPHT EVKIVEPGTC QEVQRGMQGE LCTRGYHVMK GYYKDKDATR KAINHDGWLF
TGDLAVMDED GYCRITGRLK DMLIRGGENI YPREIEEFLY QHPAVLDVQV VGVPDAKFGE
EAAAWIKLKD GKSVSPDELK AYCKGKIARH KIPRYVIFTD DYPMTASGKI QKYKLREKTI
EMFNLSSSQ
