ID A0A0J1BNW9_9MICC Unreviewed; 590 AA.
AC A0A0J1BNW9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=ABL57_19665 {ECO:0000313|EMBL:KLU08135.1};
OS Kocuria sp. SM24M-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1660349 {ECO:0000313|EMBL:KLU08135.1, ECO:0000313|Proteomes:UP000036489};
RN [1] {ECO:0000313|EMBL:KLU08135.1, ECO:0000313|Proteomes:UP000036489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM24M-10 {ECO:0000313|EMBL:KLU08135.1,
RC ECO:0000313|Proteomes:UP000036489};
RA Palermo B.R., Castro D.B., Cauz A.C., Magalhaes B.L., Carlos C.,
RA Costa F.L., Scagion G.P., Higac J.H., Pereira L.B., Almeida L.D.,
RA Neves M.S., Cordeiro M.A., Prado P.F., Silva T.M., Balsalobre T.W.,
RA Paulino L.C., Vicentini R., Ferraz L.F., Ottoboni L.M.;
RT "Draft genome sequence of Kocuria sp. SM24M-10 isolated from coral mucus.";
RL Submitted (MAY-2015) 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:KLU08135.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDNX01000168; KLU08135.1; -; Genomic_DNA.
DR RefSeq; WP_047805177.1; NZ_LDNX01000168.1.
DR AlphaFoldDB; A0A0J1BNW9; -.
DR PATRIC; fig|1660349.3.peg.2107; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000036489; Unassembled WGS sequence.
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-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KLU08135.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:KLU08135.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 431..493
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 346..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 61593 MW; 1D63D0227F82909F CRC64;
MRPSSSTVLG GRYALTDRIA IGGMGEVWKA KDRVLGRIVA VKILKEEYNG DPNFLQRFRA
EARHTALLNH PGVANVFDYG EEEGSAFLVM ELVPGEPLSN IIERRKTLDA DTVLNYIGQT
ARALAAAHAQ GLVHRDVKPG NLIITPDNRV KVTDFGIARL ADQVPLTATG QVMGTAQYLA
PEQATGQTAT GSSDIYSLGI IGYECLAGRR PFTGESQIAI ALAQVNDPPP ALPEDVPDPV
QALVMSMLAK DPKDRPATAG ALATAVDALR RGDEAAAVSA VPGMRAFLDL PDDEATQAFE
PVADAPTRLL ERDSTARAAG AAAAGAGVAA AAGPARPITA ELDVVEPSRA PGGGASAADP
VPPAGPRRER GSAWAWLLGV LLTLALLAGL LWFFLLRQPE PVAPEPTPTG TVSTTVVPEE
TTAPPADAAE TVEVLAARYE GRPVDDVVQE LSDLGFRVER QGQTSDQEEN TVLSVSPVGQ
VQRGATVTVS FSTGPDTVEL PSGMVGQQAD PLIDEIRLLG VNIIRYDEPT EDAAPGTVLR
TQPLGGSTVR PGDTIEMWVA VAPESAPTAE PSPTPSAPPT ATPTGPGQEG
//
