ID A0A1I7MKV9_9MICC Unreviewed; 746 AA.
AC A0A1I7MKV9;
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=SAMN04487966_104193 {ECO:0000313|EMBL:SFV22555.1};
OS Micrococcus terreus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=574650 {ECO:0000313|EMBL:SFV22555.1, ECO:0000313|Proteomes:UP000198881};
RN [1] {ECO:0000313|EMBL:SFV22555.1, ECO:0000313|Proteomes:UP000198881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7054 {ECO:0000313|EMBL:SFV22555.1,
RC ECO:0000313|Proteomes:UP000198881};
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; FPCG01000004; SFV22555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7MKV9; -.
DR STRING; 574650.SAMN04487966_104193; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000198881; 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; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE/THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:SFV22555.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198881};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:SFV22555.1};
KW Transferase {ECO:0000313|EMBL:SFV22555.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 453..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 477..544
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 545..612
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 613..679
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 680..746
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 322..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 79352 MW; 21C0EFD2065FAFF8 CRC64;
MSEHRTDPLI GSVLDGRYDV RARLARGGMS TVYRAVDLRL DREVALKVLY PHLAEDPALV
ARFELEAKTA ARLSHPHVVN VLDQGVDRAD GSDSEIAYLA MEYVPGYTLR TVLQRQGALT
PRIALAYLDA IVDGLAAAHA AGLVHRDMKP ENVLVSRDGR IKVADFGLAR AATHHTGTGA
TLVGTVAYIS PELVKGSPAD ERSDIYAVGI MLYEMLTGRQ PFTGASPIQV AYQHINDQVP
APSEVAPGLA EDLDELVLWC TAQEPQDRPA DAGALLTELR QIRMALADED LDFEGAVLAT
APASPGIPDD GPAGEATTVA LGASPVHPRD DDDLDEVDDP DRTEAFGPDQ TEVIGVHSTV
ALDPETTTTI PRPAAEPNGR TVPLPARPEH SPRSPAVETS ADRTQDSAPA GPLLPVAADR
ADRAPSTRQQ RRQAARAART PTEDLGQTSP RRWWIWGAVL LILAGLLSLL GWYFGSGPGG
IVTVPDVAGR SRVSAVQQLE DLGVGYTLTA AHHDLVAEDS VIETDPVAGT EVRRLTTVVV
TLSQGPQLFA VPDVSGMTQQ QAGQRLRSAG VRLGAVTHAH SDTVDEGLVL DQDPAPGAEL
RRDHRVTVVL SDGPEPVTVP DLTGLTVDQA TQALEQLGLD LEVAGSEHST EVQAGRISAQ
DPAQGQLRPG ETVQVTESLG PRLVEVPDLT DLDLEQARQL LEDAGFQVEE TTILGDVFGD
GSRVRSQNPD AGTEAEEGST VHLLVF
//