PKN1_BACSU
ID PKN1_BACSU Reviewed; 338 AA.
AC P37562; O31415;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable serine/threonine-protein kinase YabT;
DE EC=2.7.11.1;
GN Name=yabT; OrderedLocusNames=BSU00660;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- INTERACTION:
CC P37562; O34507: prkC; NbExp=2; IntAct=EBI-9303331, EBI-6667154;
CC P37562; P45870: racA; NbExp=3; IntAct=EBI-9303331, EBI-5242400;
CC P37562; P16971: recA; NbExp=2; IntAct=EBI-9303331, EBI-1535844;
CC P37562; O31435: ybdM; NbExp=2; IntAct=EBI-9303331, EBI-5255200;
CC P37562; P96716: ywqD; NbExp=3; IntAct=EBI-9303331, EBI-9302929;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D26185; BAA05301.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB11842.2; -; Genomic_DNA.
DR PIR; S66096; S66096.
DR RefSeq; NP_387947.2; NC_000964.3.
DR RefSeq; WP_009966278.1; NZ_JNCM01000028.1.
DR PDB; 6G4J; X-ray; 1.60 A; A=1-315.
DR PDBsum; 6G4J; -.
DR AlphaFoldDB; P37562; -.
DR SMR; P37562; -.
DR IntAct; P37562; 40.
DR STRING; 224308.BSU00660; -.
DR PaxDb; P37562; -.
DR PRIDE; P37562; -.
DR EnsemblBacteria; CAB11842; CAB11842; BSU_00660.
DR GeneID; 936964; -.
DR KEGG; bsu:BSU00660; -.
DR PATRIC; fig|224308.179.peg.66; -.
DR eggNOG; COG0515; Bacteria.
DR InParanoid; P37562; -.
DR OMA; FYDRGYW; -.
DR BioCyc; BSUB:BSU00660-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..338
FT /note="Probable serine/threonine-protein kinase YabT"
FT /id="PRO_0000171182"
FT DOMAIN 28..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 266..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:6G4J"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:6G4J"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6G4J"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6G4J"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6G4J"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:6G4J"
FT HELIX 257..272
FT /evidence="ECO:0007829|PDB:6G4J"
SQ SEQUENCE 338 AA; 37666 MW; 71896CE0A0A03470 CRC64;
MMNDALTSLA CSLKPGTTIK GKWNGNTYTL RKQLGKGANG IVYLAETSDG HVALKVSDDS
LSITSEVNVL KSFSKAQSVT MGPSFFDTDD AYIPSANTKV SFYAMEYIKG PLLLKYVSDK
GAEWIPVLMI QLLSSLSVLH QQGWIFGDLK PDNLIVTGPP ARIRCIDVGG TTKEGRAIKE
YTEFYDRGYW GYGTRKAEPS YDLFAVAMIM INSVHKKEFK KTNQPKEQLR SLIEGNPLLQ
KYKKALFSAL NGDYQSADEM KKDMLDAGQK AAQRKQPIKA SPQPATRQRQ QKPRQGKITK
TRYTPKQKPA KSGGLFETTL IVISVLALYF AYIIFFLI
