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Database: UniProt
Entry: A0A1I7MKV9_9MICC
LinkDB: A0A1I7MKV9_9MICC
Original site: A0A1I7MKV9_9MICC 
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
//
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