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Database: UniProt
Entry: A9FZ90_SORC5
LinkDB: A9FZ90_SORC5
Original site: A9FZ90_SORC5 
ID   A9FZ90_SORC5            Unreviewed;      1654 AA.
AC   A9FZ90;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   SubName: Full=Protein kinase {ECO:0000313|EMBL:CAN98723.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:CAN98723.1};
GN   OrderedLocusNames=sce8553 {ECO:0000313|EMBL:CAN98723.1};
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:CAN98723.1, ECO:0000313|Proteomes:UP000002139};
RN   [1] {ECO:0000313|EMBL:CAN98723.1, 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; CAN98723.1; -; Genomic_DNA.
DR   RefSeq; WP_012241162.1; NC_010162.1.
DR   STRING; 448385.sce8553; -.
DR   KEGG; scl:sce8553; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1366; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   HOGENOM; CLU_000445_34_2_7; -.
DR   OMA; SIKIQAC; -.
DR   OrthoDB; 5521237at2; -.
DR   BioCyc; SCEL448385:SCE_RS43815-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; cd07041; STAS_RsbR_RsbS_like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF01740; STAS; 1.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAN98723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW   Transferase {ECO:0000313|EMBL:CAN98723.1}.
FT   DOMAIN          7..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1533..1644
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   COILED          1472..1527
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1654 AA;  183626 MW;  5CC21450D3BA0E48 CRC64;
     MVELLNHELL ETLHDGARSS VYLGRKKSTG KMCVIKVARK GVNGTRNVAI LKRQYEITKH
     LDLDGVVRVH ELEVRLDYAA LVMEYFAGRS LRAILDGNGE GVGLAQAVRI ALQLADTLGA
     IHERNIVHKD IKPSNIIVDS DVRTSKLTDF SIASLLPGER AAVVDPWSVG EGTLQYISPE
     QTGRMNRSID FRSDYYSLGV TLYELTTRRL PFETTDPLEL VHHHIAKTPV APHLIRPAIP
     EALSRVIMKL LSKTAEERYQ STFGLKADLK ACLDMLEHGA PAADFVPGRR DKPTRLQISQ
     KLYGRQGEVG ALMAAFKDIS GSGSEGAEGG RSELVLVAGY SGVGKSAVVN EIHKPIAKEA
     GYFAAGKFDQ FTRNVPYAAI LTALREIVRQ ILTESRNELA DWRARILAAV SPNGRVIAEV
     IPEIELVIGE QPPAPALGSM ETRNRFNLTF RNFIGAIALK TRALVLFLDD LQWADTGSLN
     LLSVLLEDPD IRHLLLIGSY RDNEVDDAHP LTMMLGALRK SDARVRTITL EPLGPDHVNQ
     LVSDTLDAPR EECRELSGVI FAKTHGNPFF TIQYLESVCR EGHLRFSSET GAWRWNIADI
     QRMTVADNVV DLMVRRIQGL GEATQRVLKL AACIGNQFDL RMLALIHQKN RRATDEDLWG
     ALDAGLVVPV DGEYGIARFL DDADEDAVTF KFLHDRVQQA AYKLLTEGEQ ERIHLELGRL
     MLGESPPASV EDRIYDIVMH LNMGAKMIVD RKEREEAATL NLRAGQKARR STAYGPGVQC
     LRAAAAFLPE DSWETNHELS LAIYTDLVEL EYLTINFDRA EACAKIVVDH ARDVLEKIRV
     YETRIQFHMS QHRLADALDI ALAVLAMLEV PLCEAPPADI DIPRLAELPV LADRRMLAAN
     RILVSAFPAA VLTKPHVVPL IAFTMMEICA QHGISPSAAY AFAIYGHIQC SVMNNIDHGF
     ALGQLAIELT HRFGAIELEP KIYTLHYIAI HHWKRHLKET IEPARHAVQV GLETGDIEYA
     GYSSCQHPTY SLFAGEDLGT TEQRMTHAIE LAMKLKQQYP LYYVKIWKQL VRSLRDPSAE
     KLRLVGESFD ETSMIPCLEH NRTSLFCLHL AKGMMLYYFA EPKLAYECLR AGEEYQDAVG
     FATVVEQNLY SSLSVLAAFD RLTKEEQDAA LAKVDANQQK LGMWARHAPE NSQHKHDLVS
     AELARVGRSM IEAMALYDRA IEGARQHGYI QEEALGCELA SSFYRGMGRS EIAQHYMTMA
     YRGYALWGAD AKCQSLVAAF PHLRLEGRPD QSTSVTVTST HDDAVLDLLS VVKASQAVAS
     EIVLERLLEN LMTIVLENVG AQSGMLAVAR GDALFVEVEG TFQPKQVYVL KSAPVVSFSR
     APLSIISYVQ RTQKAILLDN AAEEARFSAD PYIREIRPKS VICAPIIRQN RLVGVLYLEN
     NLSTGVFTQN RLDLLKLLST QIAISIENAK LYERLEQEVA ARTEELRLSN EQLRDVNDQL
     QVELGERVRL QEERVQMQEA IIQTQRDRLF ELSTPCIPIT DQVMVMPIIG TIDERRAAQM
     IETAMQGVAS SSAKVVIVDV TGVKSVDTSV ASRLMSLAQA VGLLGSKAIL TGLRPAVAQS
     LVALGVDLGS IETRSNLKAG IAYAMRRTAT RLHA
//
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