ID A9GIL2_SORC5 Unreviewed; 1375 AA.
AC A9GIL2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=sce3123 {ECO:0000313|EMBL:CAN93282.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN93282.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN93282.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN93282.1; -; Genomic_DNA.
DR STRING; 448385.sce3123; -.
DR KEGG; scl:sce3123; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_006367_0_0_7; -.
DR OrthoDB; 5476622at2; -.
DR BioCyc; SCEL448385:SCE_RS16010-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CAN93282.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Transferase {ECO:0000313|EMBL:CAN93282.1}.
FT DOMAIN 12..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 274..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1375 AA; 145741 MW; 8FAB3A9C5BF71BF5 CRC64;
MLPEFTDPTD RFMIEARSRS GGMGDIFKGT DQTTGAPVAL KILRAAASPH ERARFAREIS
ILADLRHPNI VQYVAHGTWL DGRLFFAMEW LDGEDLGQRQ RRAPLGLRDS VEVVRRSAAA
MAAIHARGVV HRDLKLSNIF LVRGKGTAIK LIDFGVVKLP VPDDCPTERG TIIGTPHFMA
PEQARGEAVD ARADVYSLGA VLFRLVTGRN VFETENAIAL LSRLVVEDPP RSQQIRFDVP
EALDEVLARA IARDREQRYE NGGELARALA RVGELSNDPP ATDRSASIVR RAPAQETMPR
PAGPGDERPQ VRLANSERRV VACALFELGA GPLRPAVDAA LREVLGDDPR FEPLPDGRLA
AALGVERSRG DEAARAARAA LTVARSTPGA RASVAVGHAV RGRASLAGEA LDRAAQQLEY
AAPGAVRIDA HAIAALEGRF VVQEDARGGV IVHEDAAGFD ARKLAGLPTA PLGREHELAR
LQGIFSKIAE DGAPRAALVT GPAGIGKSRV RAELIQHLET APHAPIILLC RGDAMSQGAG
LTTLGRALRA LMGIRDGERL EDQVQKVSAH VAMRLARPLR FLAGFIGELA GVPFPDEDNE
PLRAARESPQ LMESRTRMAV EAFFRSKSET TPQILVIEDM HWADSTTVEL VDWLLGCADL
RFGVFAFARP ELSARFPSLW EHRDVTRVTL PPLSPEAADR LAASALPQAD PATRGAIVQR
AGGYGLFLEE LIRSAAEGRD GVPLSVQALV QARVDRMSSG VRGALRAASV FGQVFWTAGV
AALLERAVGA ELAELEAGEM IARQLEPRVP GQVQWTFRQA VVRDAAYASI LEEDRAALHL
AAAAWLESAG VDPGLIARHA EAGGDKARAA LLYARATRDP AASGAELDEA LELATRGLAC
GAEGTTRAAL LVRRAEILEL LGRVDEALDA AEQASRLALP GSDLWGEAQV VAATCMIEAG
QGAEGDARAA SALSPQFAAA LSPSIRAKLL ASRVRALAAL GRPAEALRAA HAAMEAARGS
GSADALLHAR EAHLAALIHA GDLAAAASLG ASLVADADGA GDAVIAARAR LNTGSALNQL
GLFEEAQELL ERALLDARGR KLRAIEGFAL HNLGMSHARL GNIEEGVALE RQASGIADAC
QISRLRFAGR LYEALFLVWR GAPGDHATAH AVARWLCEEA AHHAAALQAM ASFAMARVQL
ARRELRAAVD AAREASRHLA GGPVEEWSDA IRVTLVEALL AIGDEREANA ALDAAFSALA
ARVEALRDPR QRDAFLRGND DVGRLIALAR ERLGRSLPST ARPPHAADPS AQRAAGAPSR
SKVAKTAGAL GRKERAEAPS NNDPAAHRSA SAAQSKEAHP EGAAAAAHEK GAPRS
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