AMIN_BACSU
ID AMIN_BACSU Reviewed; 336 AA.
AC O34640;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Amicoumacin kinase {ECO:0000305};
DE EC=2.7.1.230 {ECO:0000269|PubMed:30181282};
DE AltName: Full=Kinase AmiN {ECO:0000303|PubMed:30181282};
GN Name=amiN {ECO:0000303|PubMed:30181282}; Synonyms=yerI;
GN OrderedLocusNames=BSU06640;
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=9701819; DOI=10.1046/j.1365-2958.1998.00927.x;
RA Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D.,
RA Bruand C.;
RT "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling
RT functions both in repair and rolling-circle replication.";
RL Mol. Microbiol. 29:261-273(1998).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=30181282; DOI=10.1073/pnas.1811250115;
RA Terekhov S.S., Smirnov I.V., Malakhova M.V., Samoilov A.E., Manolov A.I.,
RA Nazarov A.S., Danilov D.V., Dubiley S.A., Osterman I.A., Rubtsova M.P.,
RA Kostryukova E.S., Ziganshin R.H., Kornienko M.A., Vanyushkina A.A.,
RA Bukato O.N., Ilina E.N., Vlasov V.V., Severinov K.V., Gabibov A.G.,
RA Altman S.;
RT "Ultrahigh-throughput functional profiling of microbiota communities.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:9551-9556(2018).
CC -!- FUNCTION: Phosphorylates the antibiotic amicoumacin A (Ami), leading to
CC its inactivation. Mediates natural B.subtilis resistance to the drug.
CC {ECO:0000269|PubMed:30181282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=amicoumacin A + ATP = ADP + amicoumacin A 2-phosphate + H(+);
CC Xref=Rhea:RHEA:61588, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:144858, ChEBI:CHEBI:144859, ChEBI:CHEBI:456216;
CC EC=2.7.1.230; Evidence={ECO:0000269|PubMed:30181282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61589;
CC Evidence={ECO:0000269|PubMed:30181282};
CC -!- DISRUPTION PHENOTYPE: Knockout mutant is susceptible to amicoumacin A.
CC {ECO:0000269|PubMed:30181282}.
CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family. {ECO:0000305}.
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DR EMBL; Y15254; CAA75554.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12484.1; -; Genomic_DNA.
DR PIR; H69794; H69794.
DR RefSeq; NP_388546.1; NC_000964.3.
DR RefSeq; WP_010886430.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O34640; -.
DR SMR; O34640; -.
DR STRING; 224308.BSU06640; -.
DR PaxDb; O34640; -.
DR EnsemblBacteria; CAB12484; CAB12484; BSU_06640.
DR GeneID; 936055; -.
DR KEGG; bsu:BSU06640; -.
DR PATRIC; fig|224308.43.peg.701; -.
DR eggNOG; COG2334; Bacteria.
DR InParanoid; O34640; -.
DR OMA; LFDFDQC; -.
DR PhylomeDB; O34640; -.
DR BioCyc; BSUB:BSU06640-MON; -.
DR BioCyc; MetaCyc:BSU06640-MON; -.
DR BRENDA; 2.7.1.230; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0019202; F:amino acid kinase activity; IBA:GO_Central.
DR GO; GO:0004413; F:homoserine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Kinase; Reference proteome; Transferase.
FT CHAIN 1..336
FT /note="Amicoumacin kinase"
FT /id="PRO_0000172201"
SQ SEQUENCE 336 AA; 39338 MW; 35F73AF8D94EE40B CRC64;
MLDVHKDIKK IFHEEQVLAE AAARYGFSKD QVRFLADAEN YVYECMKDNQ PYILKITHTI
RRSSDYMMGE MEWLRHLAIG GISVAKPLPS LNGKDVEAVP DGNGGSFLLR VYEKAPGQKV
DESDWNETLF YELGRYTGSM HSLTKSYKLS NPAFKRQEWD EEEQLKLRKY VPEDQIKVFQ
QADSLMNELR RLPKSQDNYG LVHADLHHGN FNWDHGKITA FDFDDIGYNW FVNDISILLY
NVLWYPVVPY DDKAAFTEEF MTHFMKGYWE ENELDPAWLM IIPDFLRLRH MLIYGLLHQM
FDLNTIGEEE KEMLAGFRRD IENGTPITAF DFSALV
