ID B8G7P5_CHLAD Unreviewed; 598 AA.
AC B8G7P5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=Cagg_3222 {ECO:0000313|EMBL:ACL26080.1};
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL26080.1, ECO:0000313|Proteomes:UP000002508};
RN [1] {ECO:0000313|Proteomes:UP000002508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485 {ECO:0000313|Proteomes:UP000002508};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) 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; CP001337; ACL26080.1; -; Genomic_DNA.
DR RefSeq; WP_015941927.1; NC_011831.1.
DR AlphaFoldDB; B8G7P5; -.
DR STRING; 326427.Cagg_3222; -.
DR KEGG; cag:Cagg_3222; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_000288_135_2_0; -.
DR OrthoDB; 9814968at2; -.
DR Proteomes; UP000002508; Chromosome.
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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 2.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 2.
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; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 2.
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}; Kinase {ECO:0000313|EMBL:ACL26080.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ACL26080.1};
KW Transferase {ECO:0000313|EMBL:ACL26080.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 326..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 380..446
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 447..513
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 598 AA; 64907 MW; 175C821D5E249917 CRC64;
MQPQLLDGRY QIEQLLGEGG MARVYLGRDR RLQRPVAIKI PHPHLMTDPD FLSRFRHEAH
AAAMVSHPNL VDIYDVGQDG DRHYIVMEYV AGVTLKQLIN REAPFAIPRA VRIGEQIARG
LHAAHRAGLI HRDIKPQNII VTDDGQVRIT DFGVAKSHLS TAMTETGITL GTADYIAPEQ
AQGHPATPQS DIYAVGVVLY EMLTGRLPFT GDNPVAVVMK HISELPPPPR RYNPHIPAAL
EAIILRALAK DPAQRQRTAL ELAEELHNYE QLISQATVVN PQLEPSPARI PNPPRSAQIT
AARPVTIPGP RQATVRSSRQ EGLGCGVFFV GMLMLVGVLA VVFLISTGFF NNLFVNNPTR
PATTLPPGGQ STTDTPTSTL VATTTVPDLV GLSDGEARQR LEQNQLLPAP SSEHNRDVPQ
GIVITQNIPP GTVVEINSPV SYTVSLGPLL VEVPNVIGTR EDIAANQLRA AGFLVETVKE
PHPTIDTGFV IRQAPSATLR IPQGDPVTIY VSLGDVVRFP DVIGRSRAEA EAILANTPGI
ILVFVDVQGR DRIPDFDRYA PNQVVSAARE AGSSYIGLNN GDYIPRGSRI ILGVRAEE
//
