ID R4T1N8_9PSEU Unreviewed; 685 AA.
AC R4T1N8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=AORI_2304 {ECO:0000313|EMBL:AGM04892.1};
OS Amycolatopsis keratiniphila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM04892.1, ECO:0000313|Proteomes:UP000013968};
RN [1] {ECO:0000313|EMBL:AGM04892.1, ECO:0000313|Proteomes:UP000013968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM04892.1,
RC ECO:0000313|Proteomes:UP000013968};
RX PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA Ding X., Zhang L., Zhao G., Zheng H.;
RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT closing.";
RL BMC Genomics 14:289-289(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};
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DR EMBL; CP003410; AGM04892.1; -; Genomic_DNA.
DR RefSeq; WP_016332682.1; NC_021252.1.
DR AlphaFoldDB; R4T1N8; -.
DR KEGG; aoi:AORI_2304; -.
DR PATRIC; fig|1156913.3.peg.2358; -.
DR HOGENOM; CLU_000288_135_2_11; -.
DR Proteomes; UP000013968; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; 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; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AGM04892.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000013968};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AGM04892.1};
KW Transferase {ECO:0000313|EMBL:AGM04892.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 415..481
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 482..547
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 548..614
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 615..685
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 71796 MW; 8652522247EBB97D CRC64;
MTRTDPTLVG TLLEGRYRVD KLLARGGMSS VYRGVDTRLD RQVAIKIMDP RFADDRSFVE
RFEREARSAA RLHHPHVVAV HDQGFDTPGG EESGRAFLVM ELVDGGTLRE LLDERGPLDV
ALALSITEPV LSALAAAHAA GLVHRDVKPE NVLIGRGGTA LSGGVVKVGD FGLVRAVASA
GTTSSSVILG TVAYVSPEQV ATGATTSRGD VYSAGILLYE MLTGRPPYTG DTALSVAYRH
VNDDVPRPSE LRPGIPPQLD ELILRATRRD PEQRPADAAA FLAELNHLRT VLGVPAVPVP
VPLPADADRE TDAERTTPGI PAVPAVAPAS AATTVLPPVA EATLPVTGPR GTQALHREPQ
IPAAQPPRTP PPRPKPAAGD EQPGSRKRLY LMIAAAVLVL GGLIGAFAFI LNDSGPTSSS
VPKLAGMNQA AAGDALRSAK LTPAYTEEYS DTAAQHTVIR SDPAEGTALA PGATVNVVLS
KGRPIVPDIQ AGTSQQDAET AIKAAQLTPV QGEQEYSDVA KNKVIRVDPG PGSQLNIGGQ
VTIILSKGPE PLPPVPDVTG QTKDAAFQIL QQAGFQPFQA GEEFSDQFAA GQVIRTDPKG
GGKASNRRIG VFVSNAVEVP NVTFKRMEEA IQILKQAGLE PDRQGRGNGN GHGGGNGGFD
FVLEQDPQPG TKVPKGTKVK IKGFG
//
