ID A9FFI3_SORC5 Unreviewed; 1285 AA.
AC A9FFI3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:CAN94994.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:CAN94994.1};
GN OrderedLocusNames=sce4831 {ECO:0000313|EMBL:CAN94994.1};
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:CAN94994.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN94994.1, 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; CAN94994.1; -; Genomic_DNA.
DR RefSeq; WP_012237463.1; NC_010162.1.
DR STRING; 448385.sce4831; -.
DR KEGG; scl:sce4831; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_006367_0_0_7; -.
DR OrthoDB; 5476413at2; -.
DR BioCyc; SCEL448385:SCE_RS24800-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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAN94994.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Transferase {ECO:0000313|EMBL:CAN94994.1}.
FT DOMAIN 11..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT COILED 996..1023
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1285 AA; 137882 MW; 3EDFA7C45DF5C3C2 CRC64;
MRAGDVIDGR FEIMELAGAG GMGHVFRSRD LKTGEIIALK VLQNAASQDS NRLAREAQAL
ATLRVPGVVR YISHGRTEHG HPYLAMEWLT GETLSQRLAR QAFTLEESLK LARRVATTLG
SVHRLGVVHR DLKPSNLLLV GGTIDRITLI DFGVVRLSGI DQQLTMPGAI LGTPGYMAPE
QARGEAHVDA RADVFALGCL LYKCISGRAP FRGARGLAVL VKVLIEEPPS LRWLRDDVPE
ALDALVQRML SKSPEGRPSD GNAVAIELAG LMDPAAISVR PPAMSVRPPE LTTGERKVMC
LVLARDGLSA ADPSPPEIDE QARAQALSTT AARYKGQLEL VDARLPLVVL SGAGATTDLA
ARAARCALAV QALLGGAPVA VVTGRAEIAS RMPIGDLIDR VVQLLPEGRA TSRGPAIRID
EVTAGLLGAR FEITSDGGGP WLHGAREEPE APPHVLGKAT SCVGRERELA LIRDELARCI
EESTPSVVLV TGPAGIGKSR LRHELVRAIR EDGEPVEVWL GQVDPMSAGS AFGLLAHALR
RAIGLTDAEP VEERRRKVRA RVERHAALDA ARVAPFLGEL VGAPFPDDDV QLRAARRNPM
LMGDQLRLAW EDFLRAECAV QPVLLVLEDL HWGDLPTVTM VDAALRNLKD RPFMVMALGR
PEVHELFPKL WDERRGHKLR LAGISRRSSE RLVRQVLGER ESPALVATLV ERADGNAFYL
EEQIRAAAAG KGVDLPETVL AMVQAELDAL DVGARRALRA GAIFGETFSR SGVAALVGRA
EVEPLLAELE VRELIVRRSV EGAPEAAEYR FRHALVREAA YGMLTDHDRR LGHRLAGEWL
ERTGVADPMA LAEHFERGGE PARAAAATLR AAEQALLGSD LGAAIERVER GIARGASKAT
AGALRLCQAE AHLWRGEFAL AERRGTEALE RLAPGSAPWF SALTQVILAA SKRGNHDQVE
GLLRLAQGTE ARRSARPARS VCLCAGAGRL VFGGRYQLAD ELLDGIEQDA EETEQEVEVL
ARLHEARAYR AMAVGDPGAC LAGFEAALAA FEHAGDRRNA CWARNNLGSC YAELGDFEGA
DAALRASLAD AERMGLSDVR LGALLNLGPV LAQRGLVEEA QRTAEEAIAT SQRLGDARGE
GAGRACLARI VLQAGDLEGA VREARAAVAI LYGAPPLRAF AYAVLGRALL DAGQAVDALA
ATTEALCLLE SMGAEVGESL VRLSHAEALS ACGHRREAMM AIASARERLL ERARKIGDPV
WRGKFLGNVP DNVATLELER TWLEA
//
