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Database: UniProt
Entry: A0A164BJT1_9MICO
LinkDB: A0A164BJT1_9MICO
Original site: A0A164BJT1_9MICO 
ID   A0A164BJT1_9MICO        Unreviewed;       560 AA.
AC   A0A164BJT1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=pknB {ECO:0000313|EMBL:KZE89722.1};
GN   ORFNames=AVP41_02522 {ECO:0000313|EMBL:KZE89722.1};
OS   Microbacterium sp. TNHR37B.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE89722.1, ECO:0000313|Proteomes:UP000076535};
RN   [1] {ECO:0000313|EMBL:KZE89722.1, ECO:0000313|Proteomes:UP000076535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TNHR37B {ECO:0000313|EMBL:KZE89722.1,
RC   ECO:0000313|Proteomes:UP000076535};
RA   Adelskov J., Patel B.K.;
RT   "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT   Great Artesian Basin of Australia.";
RL   Submitted (JAN-2016) 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};
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:KZE89722.1}.
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DR   EMBL; LQGV01000003; KZE89722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164BJT1; -.
DR   STRING; 1775956.AVP41_02522; -.
DR   PATRIC; fig|1775956.3.peg.2521; -.
DR   Proteomes; UP000076535; 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; 3.30.10.20; -; 2.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF00069; Pkinase; 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; 2.
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:KZE89722.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076535};
KW   Transferase {ECO:0000313|EMBL:KZE89722.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        327..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          359..423
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          424..491
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   560 AA;  59308 MW;  D273144DB7915664 CRC64;
     MLSGRYRIDE LVGRGGMATV YRGHDLTLGR TVAIKILKTE LAADSAFRTR FRLEAQAASR
     MSHPAIVRVY DAGEDVETAE DGTTRAVPYI VMELVRGHLL KDIISAGPVS VADAIRYTDG
     ILEALEYSHR AGVVHRDIKP GNVMVTEQGQ VKVMDFGIAR AVSDSSSTVA ETTAIIGTAS
     YFSPEQAKGE PVDARADLYS AGVVLYELLT GRPPFRGDTP VAVAYQHVSE APVPPSDLVA
     AVPRSLDSVV LRALAKDPYQ RFADAASFRH ALDATGDGKT PTKRQVGALH SELYGANPRQ
     AAETARSLRQ LSTDTTMRRT QTGPPVAWIW TGVAVLAALL ISVFIWVIAS RPQPTLPENV
     RKVPDIVEMA WDRAEKELVA NDLEATKVEE NSDTVAAGNV IRTDPIAGTR VEPGEEITVY
     VSTGQKLATV PRLENLSRTE ATAALDDAGL TLGTVTTRND PKLAADTVIS ASLDEGAEVA
     VGTSVNVVVA SGKVTVVDMS GYSVDAAERA LEADDLGLTA NVIEDANCAG NPDAPIVKSQ
     SAVGDVAIGS TIDLVVCTGS
//
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