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Database: UniProt
Entry: A0A0X1RW82_9BACL
LinkDB: A0A0X1RW82_9BACL
Original site: A0A0X1RW82_9BACL 
ID   A0A0X1RW82_9BACL        Unreviewed;       653 AA.
AC   A0A0X1RW82;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=prkC {ECO:0000313|EMBL:AMA62795.1};
GN   ORFNames=ASO14_2195 {ECO:0000313|EMBL:AMA62795.1};
OS   Kurthia sp. 11kri321.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1750719 {ECO:0000313|EMBL:AMA62795.1, ECO:0000313|Proteomes:UP000058129};
RN   [1] {ECO:0000313|EMBL:AMA62795.1, ECO:0000313|Proteomes:UP000058129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11kri321 {ECO:0000313|EMBL:AMA62795.1,
RC   ECO:0000313|Proteomes:UP000058129};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP013217; AMA62795.1; -; Genomic_DNA.
DR   RefSeq; WP_068454994.1; NZ_CP013217.1.
DR   AlphaFoldDB; A0A0X1RW82; -.
DR   STRING; 1750719.ASO14_2195; -.
DR   KEGG; kur:ASO14_2195; -.
DR   PATRIC; fig|1750719.3.peg.2141; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000058129; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AMA62795.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000058129};
KW   Transferase {ECO:0000313|EMBL:AMA62795.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        332..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..267
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          358..424
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          425..492
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          493..560
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   653 AA;  72350 MW;  5FA967247064E349 CRC64;
     MLIGKRINGR YKLLEVIGGG GMSNVYLAHD MILNRDVAIK ILHNNFSNEE EAHRRFQREA
     LSATSLNHPN IVSIYDVGEE EGLQYIVMEY VKGMTLKQYI TQYAPLEPAR SVEIMKQLTS
     AIAMAHQNQI IHRDIKPQNI LMDEEGNVKI TDFGIAMALT ATSFTKTNSV LGTVHYLSPE
     QARGGIATKK SDIYSLGIVL YELLTGELPF SGESAVSIAL KHLQSETPSV RAIVPTIPQS
     LENVVLKATA KDAQHRYFTV EKMHEDLETV LSPERIHEPK FMIPEDHDAT RAMPAIKERP
     IPQDEDLEKT IAVSPEPTKE VTPKKKKKKK GLYVTLTILA LIIAIGLVLF MNPSIITGKN
     VEVPDVQNAT LDEAIDSLQT AGFTIGTQTA QTSDTVKEGD IVGTDPEAGS KLKKGTEVNL
     IVSSGKEKVA MQDYTGKNVD QVKTLLEKKG FKQVTVKKAY STEEYDDVIK HTPAAGKKIV
     PSATNVILTI SQGEKQNVVS NLIGFDEAAL KTYADSSGFN IKITGEDYSE NLEAGKVMSQ
     NIEAGTTLKV GSTINVVLSK GQKEKPVKLY MKKLDLDFDP EEDENGQEAS YQVVQIYLQD
     RTHNGDKVAQ EFRIKDDMEK RITLEIEEGK NASYKVLIDG EVEYEETIEY DDV
//
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