ID A9GM64_SORC5 Unreviewed; 969 AA.
AC A9GM64;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:CAN90377.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:CAN90377.1};
GN OrderedLocusNames=sce0220 {ECO:0000313|EMBL:CAN90377.1};
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:CAN90377.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN90377.1, 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; CAN90377.1; -; Genomic_DNA.
DR RefSeq; WP_012232855.1; NC_010162.1.
DR AlphaFoldDB; A9GM64; -.
DR STRING; 448385.sce0220; -.
DR KEGG; scl:sce0220; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_314930_0_0_7; -.
DR OrthoDB; 220004at2; -.
DR BioCyc; SCEL448385:SCE_RS47945-MONOMER; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.
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_repeat.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 4.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAN90377.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002139};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:CAN90377.1}.
FT DOMAIN 20..306
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 568..601
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 314..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 969 AA; 104176 MW; A804F2EA10B8371C CRC64;
MSGAQRDVFR LCGTTIDGKY RVLSAVGAGG FGVVYRGVHE GFDAPVAIKC LRLPDELSPE
AQLDFVRRLR DEGRLLLQLS RLSPGIVQAL DIGAFTTQDG ARVPYLVLEW LDGETLASHL
ERLRAGGGGA LSRREAIRLL DPAVRALAVA HEQNIAHRDV KPENLFLAEA GGARTLKVLD
FGIAKIIGDQ RSRTAALAST AEGPSVFTPR YGAPEQFDKQ RGATGPWTDV FALALVFVEL
VTGARALEGE GIVELYSVVV DPVLRPTLRA RGVSAPDAVE RVLSRALSVS PRDRYPDAGA
FWRALIAAEG LEDELPSLPP RSPPAAREAE TRVESGNARG GPAPGAEHAG TPAGIGFEPT
VPHRTDPASL RPEGAPPAPA GAEPAPRPDH GAASGEAVVV RTARDERARP GRRGLIALAL
AASAVAGAAV AVLRRPPEPP PPPSSAAVAA PEPPRPASSN PEAAALYQEA LQAYRDGAPD
VAARTMERAV ALDRGLGAGH LRVAIWTFRQ RPAVAREHFQ LALRHRAALG ERDMALLDAA
EPYVRQPSDA VAWERRLEAA ASRFPADPEL LVYLGAARFA QLRFDAAIEA YDRALALDRG
HVLAWGSKGE SLGMKGDVAA ELAAYQACAE TAPGATLCLA NRVRLLHRQG DCRQVEEHAR
RWLSIDPKAA PAHRHLALAL HARGAPRESV LVALEQGWAA VPESERRAKE LLDRISLAVL
DGDFELAVEH ARAWQREVAG RNDQDAHASP ALRLAELYRE MGLPRDAGRV ADDFLRRMSA
WSEPATTADW TIAFLPYSRR AASMTQEAYD AARLAWVERV QSKWRAAAQE IKPEHRWLLW
TEAYAAGVET AADAAAAFET MPLDQPLPSE SGRWLLLDLR IGKVYALAGK GQEAIGPLTR
VARSCAALAD PFSTTEARLY LGMALEATGD LRGAAAAYEA VLERWGKARP RSISAEQARA
RLGALRARR
//
