ID A0A0M2CRZ1_9MICC Unreviewed; 682 AA.
AC A0A0M2CRZ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=H488_0115065 {ECO:0000313|EMBL:EYT49069.1};
OS Kocuria sp. UCD-OTCP.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT49069.1, ECO:0000313|Proteomes:UP000033173};
RN [1] {ECO:0000313|EMBL:EYT49069.1, ECO:0000313|Proteomes:UP000033173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT49069.1,
RC ECO:0000313|Proteomes:UP000033173};
RX PubMed=23661474;
RA Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00172-13(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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:EYT49069.1}.
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DR EMBL; AOSQ01000035; EYT49069.1; -; Genomic_DNA.
DR RefSeq; WP_017834095.1; NZ_AOSQ01000035.1.
DR AlphaFoldDB; A0A0M2CRZ1; -.
DR HOGENOM; CLU_000288_135_2_11; -.
DR Proteomes; UP000033173; 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; 3.
DR CDD; cd14014; STKc_PknB_like; 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; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
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; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EYT49069.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EYT49069.1};
KW Transferase {ECO:0000313|EMBL:EYT49069.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 386..452
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 453..521
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 522..588
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 300..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 682 AA; 71683 MW; 32B9F400CD23FD21 CRC64;
MPGRNPVPSL INDRYEVGET IGRGGMATVH LGRDLRLGRR VAIKVLRPEL ARDGTFHERF
KREAQSVAAL NHHSIVSVYD TGEILATTDE GVDRPFIVME YVPGRTLREL IHENAVTPQE
AVDITLGILD ALEYSHRAGI VHRDIKPANV IVTPERQIKV MDFGIARAVE DTSPALTQAQ
AVLGTAQYLS PEQARGESVD ARSDLYSAAC VLFEMLTGRA PFVGGSSVDI AAQHVRDHPP
APSELDPRLG GRVDDFLAKA LAKDRSARFQ DAGQMRRALR ELRPAVPGDL DATQPLHAVR
QRDEDTKTLP PVPVPVPAGA AAPPTAAGTA VAAAPVPADD PGSGSTPARD RRRRPLRAAL
IGLLALAVLA VLGVVALQWV QDQRGGPALV AVPYVAGMDA AVAETALRNA ELVPQREEVF
DDEVPEGDAV GTDPTADTQV EEGSAVVLAV SRGPAEVEVP DDLAGRSEED VRDALEAAGL
EAGATRTANS PWVPQGMLVA TDPAGGTTVP SGSEVQLVLS TGRVTVPQLV GLSRQEAVAA
LGADAVRLSS EVVTTPRAGV PAGQVVDQSV DAGQSAPQGS TITLTVAVAP EPEPAPEPSP
SPTPSPSPEA TEDEEEAEET AAPEEEESEP GSTPDDSAET SPEDSPETEA RDDDEQDGIP
EQAADRAREA LEQGADRGPR RD
//
