ID A0A1H4K6M7_9MICO Unreviewed; 596 AA.
AC A0A1H4K6M7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04489806_1032 {ECO:0000313|EMBL:SEB54047.1};
OS Microbacterium humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=640635 {ECO:0000313|EMBL:SEB54047.1, ECO:0000313|Proteomes:UP000199183};
RN [1] {ECO:0000313|EMBL:SEB54047.1, ECO:0000313|Proteomes:UP000199183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21799 {ECO:0000313|EMBL:SEB54047.1,
RC ECO:0000313|Proteomes:UP000199183};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNRY01000001; SEB54047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4K6M7; -.
DR STRING; 640635.SAMN04489806_1032; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000199183; 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-KW.
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; -; 1.
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:SF32; SERINE/THREONINE-PROTEIN KINASE PKAA; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 1.
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:SEB54047.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199183};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SEB54047.1};
KW Transferase {ECO:0000313|EMBL:SEB54047.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 339..358
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 391..457
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 61999 MW; 808FD1F78ABFCC91 CRC64;
MRPMAGVTFG GRYELESRIA IGGMGEVWKA TDNVIGRTVA IKILKDEYMG DPGFLERFRA
EARHAALVNH EGIANVFDYG EENGSAFLVM ELVPGEALSS TLEREHVLST DATLDIVAQT
AGALQAAHAA GLVHRDIKPG NLLITPDRRV KITDFGIARI ADQVPLTATG QVMGTVQYLS
PEQASGHPAS PATDIYSLGI VAYECLAGKR PFTGESQVAI AMAQINEAPP ELPATVAEPV
RNLVFSMIAK NPDDRPASAA HVVRAANALR RGDIAAATAA VPAVSEGTGG TSIVPSGNDQ
ATQLLSEHTD TGTAALPVAG AEGDEETGKK KRSPWTWPLI VLIAVLILVL GGTILALVNQ
DNTGDTPATN TATRSSTPPK TPSQEPTPED TRVDIVESDY VGRPYDDVAA ELQTLGLKVE
KKVGATATSG EQVDKVTDVS PYGKVDPGTT ITLTVYGPLA TPNAPSNAPS VNNCTGGGCQ
FAASESNKTV SVTWDAYSNC PTGTSVTGYR LHINGGSAKS TDIDPGGNQN VPVTIDDGAN
QLTVSWSVFC GEAESAQSPN TITTVTWDDS SSTPAPGDEG TSQGLPGAVG VLPSRR
//