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Database: UniProt
Entry: W0ZBJ0_9MICO
LinkDB: W0ZBJ0_9MICO
Original site: W0ZBJ0_9MICO 
ID   W0ZBJ0_9MICO            Unreviewed;       568 AA.
AC   W0ZBJ0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=MIC448_460061 {ECO:0000313|EMBL:CDK01124.1};
OS   Microbacterium sp. C448.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK01124.1, ECO:0000313|Proteomes:UP000028883};
RN   [1] {ECO:0000313|EMBL:CDK01124.1, ECO:0000313|Proteomes:UP000028883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C448 {ECO:0000313|EMBL:CDK01124.1,
RC   ECO:0000313|Proteomes:UP000028883};
RX   PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA   Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT   "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT   Microbacterium sp. Strain C448.";
RL   Genome Announc. Announc.2:e01113-e01113(2014).
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:CDK01124.1}.
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DR   EMBL; CBVQ010000210; CDK01124.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0ZBJ0; -.
DR   STRING; 1177594.MIC448_460061; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000028883; 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-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 2.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 2.
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:CDK01124.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028883};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CDK01124.1};
KW   Transferase {ECO:0000313|EMBL:CDK01124.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        333..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          365..429
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          430..497
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   568 AA;  59391 MW;  08FB32C26B818C82 CRC64;
     MTNEPRVLSG RYRIDELVGR GGMASVYRGY DLTLGRAIAI KMLKRELADD AAFRTRFRLE
     AQAASRMANP TIVRVFDAGE ETERDGDGST HPVPYIVMEL VEGALLKDVI DAGPVPEADA
     VRYVDGILEA LEYSHRAGVV HRDIKPGNVM ITDAGQVKVM DFGIARAVSD SSSTVADTTA
     ILGTAAYFSP EQAKGEAVDG RADLYSTGVV LFELLTGRAP FRGESPVAVA YQHVSETPDA
     PSELNPDVSR ALDAVVLRAL AKDPFQRYQS AEQFRGALSA AVGGAAPSKR QLGALTTELY
     GANPRQAAET ARSLRQLSTD DTMARTQSGP PAAWIWTGVA VLAVVIISLF FWIVTIQPQS
     EVPSTARVVP SVVGQTYEAA NSALAEADLN AVRRDEASDT VSEGSVVRTV PAAGVGVTVG
     QDVTVYVSTG AETTPVPPLE GLSEADARAA IEAAGLTVGQ ITSRSVPGKG EGTVISSSPV
     AEESVIVGST VNLVTATGRV PIINYVGFTL QAATDSITGP SIQLTVSRIE DPSCVATDPE
     IVTQQSIPPG EAAVGSTIAL TVCTGVAP
//
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