ID A0A259U0Y6_9BACT Unreviewed; 860 AA.
AC A0A259U0Y6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BSZ36_12120 {ECO:0000313|EMBL:OZC03659.1};
OS Rubricoccus marinus.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubricoccus.
OX NCBI_TaxID=716817 {ECO:0000313|EMBL:OZC03659.1, ECO:0000313|Proteomes:UP000216446};
RN [1] {ECO:0000313|EMBL:OZC03659.1, ECO:0000313|Proteomes:UP000216446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-29 {ECO:0000313|EMBL:OZC03659.1,
RC ECO:0000313|Proteomes:UP000216446};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
RL Submitted (NOV-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:OZC03659.1}.
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DR EMBL; MQWB01000001; OZC03659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259U0Y6; -.
DR InParanoid; A0A259U0Y6; -.
DR OrthoDB; 9813021at2; -.
DR Proteomes; UP000216446; 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; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13432; TPR_16; 3.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 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}; Reference proteome {ECO:0000313|Proteomes:UP000216446};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 554..587
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 588..621
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 622..655
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 656..689
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 690..723
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 860 AA; 91962 MW; C94BDDE4788CA3F2 CRC64;
MTASPPASGA SPDDGSFLVG RSVGPYRIEE RIGGGGMGVV YRATDTRLGR TVALKFLAAR
LRADPTARQR LREEARAVAA LDHPHVASVF DVGETEDGRE YVAMAFYEGE TLEARLQQGP
LAPEAAVEIA CQIASGLGAA HRAGIVHRDV KPANVMLVGE PASAKVLDFG IAKTEHVHLT
QEGESVGTAL YMSPEQLRGE PTDARSDVWA LGAVLYEMLA GRRPFGGSYA AAIGYAVLHE
DPPPLAGDLP DGLEAVVLRC LAKSPEARYA SMEALAADLD AFQDGRVPPA PEATPARAGT
GLWRWAAALL AVVLVAIAVV VLWPEPARAE SQRLVVLPFR ASGPDAEALS EGLVEAVTSK
LGALGPLRER VRVVPASEVE AGMTPSEAHE RFGATLVVEG SVATEGDEVR VTFGLVEVGR
EGPVQGPTEQ IDDARGSSFA LQDAAALGVL RMLRIEIGAA EKSALASGGT GDPEANERYL
RGRGVLRNQQ SDADVARARD LFGEAISRDP AFALAYAGLA EAEWQTYRRT DAVEWADRAI
ANAKHALELD DGLAEVHISL AIIYQGRQRF RDGLASIDRA LEIDPTNGEA VRRQAKIYAD
LGRAPEAERA FRRAIALAPD LWRPYNSLGV FYLDEGRAAE AAAQFQKGLE INPVNLSLFI
NLGVASVISG DFEQAQRAFE EVLRLDPDDS DAAYNLSTVR AFLGDTGGAV EAAQRAVALR
PDDYEAHEAL AEALWNAGKQ GEARASFQTS LRLARGHLTV GRDPDVLKVM ARVFALSGQR
DSARVYLREI GERISPEAAS VQEVFVIGVT HELAGQRAEA LSWLRSALDR GFGAEQIKRS
PWLGDLREDP LAISLLTPDP
//
