ID A0A1R1M2X5_9MICC Unreviewed; 706 AA.
AC A0A1R1M2X5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BGP79_03090 {ECO:0000313|EMBL:OMH34152.1};
OS Tersicoccus sp. Bi-70.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Tersicoccus.
OX NCBI_TaxID=1897634 {ECO:0000313|EMBL:OMH34152.1, ECO:0000313|Proteomes:UP000187343};
RN [1] {ECO:0000313|EMBL:OMH34152.1, ECO:0000313|Proteomes:UP000187343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bi-70 {ECO:0000313|EMBL:OMH34152.1,
RC ECO:0000313|Proteomes:UP000187343};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Tersicoccus sp. strain Bi-70.";
RL Submitted (AUG-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};
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:OMH34152.1}.
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DR EMBL; MIEU01000011; OMH34152.1; -; Genomic_DNA.
DR RefSeq; WP_076694099.1; NZ_MIEU01000011.1.
DR AlphaFoldDB; A0A1R1M2X5; -.
DR STRING; 1897634.BGP79_03090; -.
DR OrthoDB; 9762169at2; -.
DR Proteomes; UP000187343; 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-EC.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
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; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..285
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 436..502
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 503..569
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 570..638
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 293..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 706 AA; 72835 MW; 3DC6FDC569A47296 CRC64;
MSEARLLNDR YRVDGLIGRG GMADVHAGHD TRLGRPVAIK LLRSDLARDP SFQSRFRREA
QAVAALNHPN VVGVFDTGEE LIVDAAGRAV DAPFIVMEYV TGHTVRQLIT DERLTIGTSL
AHADGVLSAL QYSHDAGIVH RDIKPANVMV TDEGAVKVMD FGIARAIEDS SATLTQTQAV
LGTAAYLSPE QARGERVDAR SDLYSAACLF YEMVTGRPPF RGDSAVSVAY QHVRELPPAP
STLNPDVTPA IDSVLLHALE KDRQDRFQDA AEFGEALRAA AHGVVYQPLV TGVDEDTLQM
PPSSASDTPR EREGRDRTAV GAAAGAAAGS GLAAAALAGG SPTASTDATA TEALGRPDQA
GASPATTALT SADDDEDPSG TDAAPLVLGI GTDDEVHPDT RARRRAWLIT GIIALVLVLG
AVAVYFTNLL VARSAPPEMV TVPAVANMSQ ADASTTLANA NLRIRLDRTN STTVKNGDAI
STDPHSGTRV SPRSEVTLLV SSGPARVTIP SDLAGRPADQ VRDELRQLGL DPLQTTTQNS
ATVDEGALIN TVPALGKQVP AGSRVDLVIS TGRVTMPQVV GLTEAQARAK LSAADVALPV
RIETAENAVV KPGTVTAQSA PANGNVDQGT TVTLTVARAP AKASPSPTPS PSSPSPSPSP
TSKPSASASP TPTPTPSTSS SSSAAGPGQG TGRSGAPGQQ KKDQGG
//
