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Database: UniProt
Entry: A0A1H4K6M7_9MICO
LinkDB: A0A1H4K6M7_9MICO
Original site: A0A1H4K6M7_9MICO 
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
//
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