ID   A9GH81_SORC5            Unreviewed;       856 AA.
AC   A9GH81;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   02-SEP-2026, entry version 104.
DE   RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027};
DE            EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027};
GN   OrderedLocusNames=sce6257 {ECO:0000313|EMBL:CAN96424.1};
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN96424.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN96424.1, 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AM746676; CAN96424.1; -; Genomic_DNA.
DR   RefSeq; WP_012238878.1; NC_010162.1.
DR   AlphaFoldDB; A9GH81; -.
DR   STRING; 448385.sce6257; -.
DR   KEGG; scl:sce6257; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG5616; Bacteria.
DR   HOGENOM; CLU_013589_1_0_7; -.
DR   OrthoDB; 9797180at2; -.
DR   BioCyc; SCEL448385:SCE_RS32130-MONOMER; -.
DR   Proteomes; UP000002139; Chromosome.
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; 3.40.50.10610; ABC-type transport auxiliary lipoprotein component; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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_rpt.
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; PF00069; Pkinase; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00028; TPR; 2.
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; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00159};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW   Serine/threonine-protein kinase {ECO:0000256|PROSITE-ProRule:PRU00159};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}.
FT   DOMAIN          34..292
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          647..680
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10027"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   856 AA;  91660 MW;  22DAF72BF41AF25B CRC64;
     MSDRRLTASE PTPRSEPSHG SGFVAAPQRI AGRYEILGLL GSGGMGSVYR VRDVELDEVV
     ALKMLRRDLA DSAGMLERFR QEVKLARRVT HRNVARTFDF GDHDGEKFLT MECVEGESLH
     SVLARTGPMP SQQAIGIGCS LCDGLGAAHA AGIVHRDLKP ENVLIDRNGR VVITDFGIAR
     TSSGPSAGES QGFVLGSPAY MSPEQLTGEP DLDARTDIYA LGMILFECLT HRRAWPGAGA
     IAAAMSRLKS PPPDPRSVRP DVPLVVADVV LRCMAIRRED RYASAAEAHR ALLLARSRLS
     IAPQPAQSLV SAIAASSATA APTAPQPIEQ NPTRVAASPV EALTAPQRRL NSPTLAAPAP
     TPAPTPTSSL KTVAVLPFRN VGAPDDEYLA DGFTEDLTDT LSMTAGLKVR PRAAVSRVRL
     DGRDPRDVGR ELGVQVVVEG SIRRTGGGGY APDGPRSQPP APYSRPASRT PPGGVRVTVR
     VIGVEDGFQL WAKRFDSSPE ALLTVSDDAA GAIAAALTVD AASRERESPS DPRAIDLYLR
     ARHQMRRLWY GDAAPAVALF EEALSFSPND PSILSGYAIA FARLMGARGE GAAQFAKAQQ
     AAERAIALAP ALGEPWVALA TVRFSAGDPV GAVPALRKAL QCAPSLAKAH ELLGRILLEA
     GLVDEAMFRL DTALALDPSE PFPRWELARG RALLGDWPAA GVLLDLPAED PSSRFHKAVM
     RARFGLWRGA AFPIDDLSLA TETIPIQYAR IYRDVLATSR LSDEQRALLS AKADSSEPGS
     RLRPLFFQMY AEILAFLGED DALFRVLAGA VDAGLFDAFW MQRCTVLDRA RADARFAPLR
     ARVEERAAAI IAAFRG
//