ID I3CHJ6_9GAMM Unreviewed; 879 AA.
AC I3CHJ6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=BegalDRAFT_2233 {ECO:0000313|EMBL:EIJ43089.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ43089.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ43089.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ43089.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) 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; JH600070; EIJ43089.1; -; Genomic_DNA.
DR RefSeq; WP_002689993.1; NZ_JH600070.1.
DR AlphaFoldDB; I3CHJ6; -.
DR STRING; 395493.BegalDRAFT_2233; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG4252; Bacteria.
DR HOGENOM; CLU_015582_0_0_6; -.
DR OrthoDB; 9816047at2; -.
DR Proteomes; UP000005744; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007890; CHASE2.
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 PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00220; S_TKc; 1.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EIJ43089.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW Transferase {ECO:0000313|EMBL:EIJ43089.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 610..871
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 579..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 879 AA; 98704 MW; 2AED4AEF387FA774 CRC64;
MTTFKEKLAM NDWIIGVLVA VCLLGLAQFG FLQPLENILY ANGMRYTSQH TNDKVAVIAI
DTNSLEQLGA GQWSRTTYAQ LLDILQPYAD VIATNLDFSK PQQDAGTERL AELIRFYSES
PAINQLPTEL AKLNTLIATV TKVRRNRASE RDSLAELNDF AQSAKLWTEL PNILTTLEDK
LNAAYSELDA DGIFAERLKK SGKWVFAVPF TLGEPLLPQS DLPDSITRNR LTNISERFDT
ARPSPQPLSI NTIRSPLERF NENTSVLPDL LLLDNRVPLV TQYQQLYLPS LPLLLAAKHL
RVNLQDIEIR LGQGVRLGAL RINTDANLNI QPIFYHEHEI ARQSAFTLDS FVDVLRGNIS
PEKYRDKVVL IGMTAPNYST RQMTPIGEMP PILTIAHSVS SLLNQNYLIT PHWAVGLQTA
LFLLILIYLC LILPHLKPKI ALLISFISFI TLLVLYFGLL RLGLSISCTL PLLLLSLGHL
LLTSKRGIMA YQDVFRMLPN AVESNRLLGL AFQGQGQLDM AFEKFRLCPT DEGILGLLYN
LALDYERRRQ ARHAAAVYRY ILSHAPNFRD TERRLERLQS TRKPRLRGTN NHLDDWLQDE
SGEKPQLGRY QVERQLGKGA MGVVYLGKDP KLNRLVAIKT LPLSQEFEAE DLPEATARFF
REATAAGRLK HEHIVAIYDA GEEYNLAYIS MEFFKGGNLT PYTKTEQRLP IADIIDIGYQ
AATALNYAHN QGVIHRDIKP ANIMYNPATK KIKITDFGIA RITDAKRTKT GIILGTPSYM
SPEQLAGKMV DGRSDLFSLG ILLYQLLTSV LPFQADSMAT LMYKITTEPH PDLSMLRPDI
PTCLQDLINK ALAKDPEDRF QTGAEFAAAL RDCKVTSCA
//
