ID A0A0H2KT61_9MICO Unreviewed; 688 AA.
AC A0A0H2KT61;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=FB00_00410 {ECO:0000313|EMBL:KLN36348.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN36348.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN36348.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN36348.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-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:KLN36348.1}.
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DR EMBL; JNBQ01000001; KLN36348.1; -; Genomic_DNA.
DR RefSeq; WP_047230888.1; NZ_JNBQ01000001.1.
DR AlphaFoldDB; A0A0H2KT61; -.
DR STRING; 264251.FB00_00410; -.
DR PATRIC; fig|264251.5.peg.80; -.
DR Proteomes; UP000035265; 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; 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:KLN36348.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000035265};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:KLN36348.1};
KW Transferase {ECO:0000313|EMBL:KLN36348.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 390..457
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 458..525
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 526..588
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 598..661
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 328..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 688 AA; 70442 MW; E29B538CB682A8D1 CRC64;
MVDNAPRVLA GRYQVGELIG RGGMAEVHIG HDNRLGRTVA IKILRSDLAR DPTFLARFRR
EAQAAASLNH PAIVAVYDTG EDVHADATGN SVHVPFIVME YVEGHTVRDI LRDGQAVPID
EAVEITAGVL AALEYSHHAG IVHRDIKPAN VMITPTGAVK VMDFGIARAM ADSAATMTQT
QAVIGTAQYL SPEQARGETV DARSDLYSTG CLLYELLTGR PPFIGDSPVA VAYQHVREAP
ATPSAVAPDV PEVLDRITLK ALAKDRTARY SNAAEFRADL ENAVRGGAIT APALGVAAAA
AGLGAAAAAA DLQPTMVESA TQVMAPAAAA PNPWATSVAP AVPPGDEVPG EDEEEPKSRK
GLMWTLIAIG VLALAAIITM LVINGQGEDE PTTGTVPTLS AGVTPEEAEQ RITDAGFAYE
QAIDQESTEA EGTFTKTDPA GGTEADLGST VTAFFSAGPD AVVIQDVKGK SQDEARQILE
AQGLEVTSGG SEDSKDVAKD AATRTDPAAG QSVAGGSTVT LYVSSGLVAL PELVGDQRQS
AEQKITDLGL KPVVNEVESD EPEGQVVAQR PNAGSVPQGS EVTIDVAIPK AEEPETTNVP
RNLVGMTLDQ ANDALGGAGL NPGTQQNQES DQWPAGVVIG SDPGGGTEVE VGTEVSLIVS
TGPGPSTGGD NGGGGNNGGG NGGGGGEG
//
