ID A9GEU8_SORC5 Unreviewed; 1501 AA.
AC A9GEU8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:CAN93059.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:CAN93059.1};
GN OrderedLocusNames=sce2900 {ECO:0000313|EMBL:CAN93059.1};
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:CAN93059.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN93059.1, 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; CAN93059.1; -; Genomic_DNA.
DR RefSeq; WP_012235531.1; NC_010162.1.
DR STRING; 448385.sce2900; -.
DR KEGG; scl:sce2900; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_004254_0_0_7; -.
DR BioCyc; SCEL448385:SCE_RS14885-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-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; IPR003593; AAA+_ATPase.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
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; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR PANTHER; PTHR32071:SF95; TRANSCRIPTIONAL REGULATORY PROTEIN ZRAR; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 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.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:CAN93059.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:CAN93059.1}.
FT DOMAIN 15..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1198..1423
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT REGION 285..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1147..1174
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1501 AA; 155929 MW; 902EE70B79BF1842 CRC64;
MSEPSTVTPR LAERFRLLDI AGSGGSAEVW RAVDQERGGV VALKIEPRER GASAAQRASV
RRVLGREALH AALALSPRLP ELVDVGWLAA PSGVARAARA EGAPGEEGRA FVAMRWIEGR
AVADALRGLP PGERAALALA AARDAGEALA DLHGIGLAHG DLKPENLILT PEGRIAVIDL
GLACSIHETS VDGATLRYIA RGDAELGDAR ARDLLALGTL LAEIAFPGVA DADDPIGAAR
AAAAAESAAG PPLDAICRAL LSPSPAARPS SAWVTESARA AIAGGRRARP PFAAPPAGRA
GRDAGAPGAE RDRQDRDARR VRAAYLRLRR HELEAALGVR DDVAPWLVDA FAVVERVRAL
SGASLRAGDG AARVGPPQSD AAWLGRLGPD RVARWLTALA GTSATAWPMG PLASAPERAL
ADALVALARQ VPPRAWTFAD VEAAVLGTPG SGARRRASAG PEDRGAAEGA AEAQAIGAAE
AAALALAIAR VPPDPLALEA IEQRDDAPAS LVVAAANALR LHGDAGRARS LMLRSCVRGA
TEAAALAAEV LRRAGDRALA EERARAAIDA GADPEGRARA VLARVAIDAG ALEAADALAG
DAVTAPLCEV RALLAVLRGD TARALSEVAR GEALASSVEE LARMAAVRGY AWHASDPERA
HASFSAAVDY AVRAGAVVEE ATYRTGEAAA AVDLGDLDGA IATSTRAALL WEHLGRPAQG
ARALLACAAA YATAGLVHET CRTAEDAIAR ARDAGDAKAE AYALWAIADV VAARGDGVVG
ADVGSHVDPR AAAARAAALL AGGSADDTLR AAARLLRHGA GELDGARVEE LDELANGPEP
AAASRLDWWG ARAAIALAAD DVGAASAADD APRGPAGASG ASASRGRSDR VLAAIAALAG
ARAPIAARGP ALAAAHALAV RAGQTDVAHR VLAALADAAR ELCGRTAGAG SAGASAASPG
ASALSGAVRS LPWVVRARAM PESGLRPEQA RDLEALVGAL GERERLAPLL DRVVDALVLW
TGVERGLLLL RAPNGRLVPR AARNLARSRL GAEQLALSET LARRALEARE PVVAVDAAGE
LPSVHHSVHA LKLRSVLAVP LVARGEALGV VYLDDRVRRG AFGAQELRWA RAIASVAALA
ISDARAQVEL RRAARRAERA SSRLAEELAR REAELDAAAL ELARARGGRD TRYRYDAIIG
ESEPLRAMLR LVDRVTASEV PVLVCGESGS GKELVARAIH HNGPRAAHAF VSENCGAIPE
GLLESALFGH VRGSFTGADR PRAGLFEVAD RGTLFLDEIG EMSLAMQTKL LRVIEDGLVR
PIGSERARKV DVRVIAATHR DLAALVRARA FREDLLYRLN IITIRVPPLR ERATDVPLIV
QHLVEKHSRG PVRVTRGAME RLSACAWPGN VRQLENEIRR AIVLCDGTID REHLSPEIAH
GGNATPRELG LNVRARIDAL ETELVRDALE RTRGNQTQAA KLLGLSRFGL QKMIKRLSIE
A
//
