ID Z9JQC2_9MICO Unreviewed; 737 AA.
AC Z9JQC2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BF93_08445 {ECO:0000313|EMBL:EWS79952.1};
OS Brachybacterium phenoliresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS79952.1, ECO:0000313|Proteomes:UP000023067};
RN [1] {ECO:0000313|EMBL:EWS79952.1, ECO:0000313|Proteomes:UP000023067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS79952.1,
RC ECO:0000313|Proteomes:UP000023067};
RA Wang X.;
RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL Submitted (FEB-2014) 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:EWS79952.1}.
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DR EMBL; JDYK01000021; EWS79952.1; -; Genomic_DNA.
DR RefSeq; WP_038374023.1; NZ_KK070004.1.
DR AlphaFoldDB; Z9JQC2; -.
DR STRING; 396014.BF93_08445; -.
DR PATRIC; fig|396014.3.peg.3190; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_11; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000023067; 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; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
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:EWS79952.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000023067};
KW Transferase {ECO:0000313|EMBL:EWS79952.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 403..469
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 470..537
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 538..603
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 606..671
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 568..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 737 AA; 76461 MW; 70F5EEC2806DF1E8 CRC64;
MNADEFVLSG RYRVGRLLGH GGMAEVYLAE DTRLHRTVAV KILRSDLARD ATFQERFRRE
AQSAGGLNHP SIVSVYDTGE DTSRDAAGNE IGVPYIVMEY VEGHTLREYI DPENPMDAAQ
AVRITTALLS ALEFSHDAGI VHRDIKPGNV MITATGAVKV MDFGIARAVA DAASAMTQTQ
AVMGTAQYLS PEQARGQLVD NRTDLYSAAC VLYEMLTGRP PFTGDSPVSI AYQHVREAPQ
APSVFNPAIT PEMDQVLLTA LAKDREARYP SAAEFSRDLQ AVVGGRTPQL VGGAAARSAG
AASDAETTTV LSAADLPTEA LSPTRTTGRH AAVAGGAAGA GYAAGSAASP LDGGTGPLAA
QDGQLVAEEK HRRPVWLFVL VAIAVLAVIG ASLAILRPWD PPGPETVTVP TLTGLNSDQI
TVKLDEVGLT PAFESVSSTE VDKGLFISSD PAPGESAETG DTVNVTLSSG PADTEVPDVS
GKTRADAEQL IRDAGLEPAY QADEDVAKAE AGTVTRTNPR AESPVTQGTQ VQFWVATGNV
AVPQLVGLDE ESAKKAIEDA GLVADVQDQE APDEEPGTVL SQNPTSASNP VANGSTVQIF
VARERGPVTV PNVAGDTLDN ARTRLSEAGF GMNPPQYEPS DSVAEGVVIR TDPEGNEQAE
YGSSVTVVVS SGPEQTTAPT PTENPTTPST EPTTPTPDQE DPTTEPSADP TTDEAAPGNG
NGNGSGNGNG NAAGGRG
//
