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Database: UniProt
Entry: A0A3N9UFQ1_9BACI
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ID   A0A3N9UFQ1_9BACI        Unreviewed;       658 AA.
AC   A0A3N9UFQ1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Stk1 family PASTA domain-containing Ser/Thr kinase {ECO:0000313|EMBL:RQW75009.1};
GN   Name=pknB {ECO:0000313|EMBL:RQW75009.1};
GN   ORFNames=EBB45_08505 {ECO:0000313|EMBL:RQW75009.1};
OS   Lysinibacillus composti.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=720633 {ECO:0000313|EMBL:RQW75009.1, ECO:0000313|Proteomes:UP000274033};
RN   [1] {ECO:0000313|EMBL:RQW75009.1, ECO:0000313|Proteomes:UP000274033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A12701 {ECO:0000313|EMBL:RQW75009.1,
RC   ECO:0000313|Proteomes:UP000274033};
RX   PubMed=23812821; DOI=10.1007/s12275-013-2664-1;
RA   Kim S.J., Jang Y.H., Hamada M., Ahn J.H., Weon H.Y., Suzuki K., Whang K.S.,
RA   Kwon S.W.;
RT   "Lysinibacillus chungkukjangi sp. nov., isolated from Chungkukjang, Korean
RT   fermented soybean food.";
RL   J. Microbiol. 51:400-404(2013).
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RQW75009.1}.
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DR   EMBL; RRCT01000006; RQW75009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N9UFQ1; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000274033; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 3.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.40.2560; -; 1.
DR   Gene3D; 3.30.10.20; -; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF03793; PASTA; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF21160; PrkC-like_PASTA-like; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:RQW75009.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000274033};
KW   Transferase {ECO:0000313|EMBL:RQW75009.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        342..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          365..432
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          433..500
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          501..568
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          307..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   658 AA;  73044 MW;  474CAA1965C775E4 CRC64;
     MLIGKRINDR YKILQLIGGG GMSNVYLAYD MILNREVAIK ILRYDAANEE EFHRRFQREA
     LSATSLTHPN IVSIYDVDED DDMHYIVMEY VKGKTLKQYI NEFSPLSPAR SIHIMKQLTS
     AIAHAHENHI IHRDIKPQNV LVDQEGNLKV TDFGIATTSS ATSYTKTNSV IGTVHYLSPE
     QARGGIATKK SDIYALGIVL YELLTGELPF SGESAVSIAL KHLQAETPSV RAFDANIPQA
     LENVVLKATA KNEAHRYDSV EEMQEDLDTV LSPSRSNEHK FMPPVDDDAT KAIPIIKDRM
     PVNEIANTKV LASSTGKKPK DKSSTGKEKS EKTVKKRSRK KIAAIITATI AIIILLMILL
     FNLLSPKTIE IPDVANMEPE EAKETLEKAG FVIGKEREQN SDDVEEGLVI KTDPKAGLTR
     VEGTKINLII SIGNEEIEMD DYIGQGIDQV TTVLNNMDFK DIELEYEHSD QPAGTIIGQS
     PEAGEKVVAE DTTVTLTISE GVRYVTVPDL NGFNQTAISE YERNTGLNIE VSSEEHSDTV
     PAGSVISQDP HANAQVQEGG TVKVVLSKGP APKQVKMYVN SIVIPYEPIE LGVPQVVEIY
     IEDKNRRMSE PVETIEITED YTYKIQLEIE EGQKAAYRIV RDSMEISKAT ISYDELKE
//
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