ID   Q7UEH2_RHOBA            Unreviewed;      1899 AA.
AC   Q7UEH2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=RB11334 {ECO:0000313|EMBL:CAD79064.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD79064.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD79064.1, ECO:0000313|Proteomes:UP000001025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC   {ECO:0000313|Proteomes:UP000001025};
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294153; CAD79064.1; -; Genomic_DNA.
DR   RefSeq; NP_869921.1; NC_005027.1.
DR   RefSeq; WP_011123208.1; NC_005027.1.
DR   STRING; 243090.RB11334; -.
DR   EnsemblBacteria; CAD79064; CAD79064; RB11334.
DR   KEGG; rba:RB11334; -.
DR   PATRIC; fig|243090.15.peg.5498; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_235836_0_0_0; -.
DR   InParanoid; Q7UEH2; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000001025; 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; IBA:GO_Central.
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; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_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   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00320; WD40; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CAD79064.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Transferase {ECO:0000313|EMBL:CAD79064.1}.
FT   DOMAIN          384..677
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          546..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1899 AA;  211076 MW;  BFE247C16D8A3F42 CRC64;
     MTEKPGMQFF LAKDGSKEGP LTSKDLRKLS AEGKLKPDDL IFIDNQSKPV RARRFSGLFT
     NVATNTKQLK KGSRRFNITK RSVFISCVTH EFRHYRDLLA ARLSLPGVEV RHQESFIDSG
     TTTLGKLKEY ISTCDAVIHV IGDSTGSYPT AAEVGKLRSE LDKFGSTFDL SELEKPPGIS
     YTQWEAWLAI YYDKPVLIYK AADLASRSPE FAFNQEQKER QRIHWRLLEA NGRDRREFAS
     AEELVIEVLR SLLIVVPDIK QNVGQGDFRD RNLLFGVLAL QDALISREAF VRACGLWAMD
     TGQSLSELLE SEGIINRSDR VLVEARLERK ILAKGGDPRK SLADAIDNDI RLTLSESLDP
     QTIASLPDQS HFLKTQLSPE HWRYRLTRTH QTGGLGVVSV AEDTVLNRNV AIKQLKGNRA
     IDPMAIERFL REARITGRLQ HPNIIPVYEL GLTPDDQLPF YAMRFVGHKT LHDAIRHHHL
     DRTASERAKK VHFRELLQSF VSVCKAVAYA HSEGIMHRDI KPANIMLGDY GEVILLDWGL
     AKRIGDEEPD QSQKRDVEGK SDDSGFDQTR AGTRLGSPGY MAPEQASGRI SDHGAHTDIY
     GLGATLYELI AGDLPFKASS TASLMEAIQH QSIPSIAESN KQVPAALVAI CGKAMEKLPA
     DRYASAEALA DDIQNWLADE PIAVLPDNLL RASQRAIRKR PSWVSGTIAA LAVGVLTVTT
     GLFFVNKEKN LKNESLTRES ELRRVAVANE SRATKSLELA ETRLETIVGQ RTEIDLATAQ
     TYLATSQELY ANGQFDHAAR LLLPAFRLSE ASNKLKQAVS DTAAFQFTHG GKQAVPLARF
     KSPILQVSSS QDGTKIAVLQ DNSRIVFVID PKSMTVNGSF ECESVVQRVL MNAAGTHLLI
     AVEDGKVLYQ ALSDPKDRTA LLDTPSDCTQ LQFGARDSIA YVGTLDGLLK YDLRSGRLLA
     RCKTEFRCDA IVPSKDGNVL YISGRQDRID WGGLKLVGTI KGNGLSLQAN LAAKRGFYLE
     RVDAERFIVE KTMINDGALS WPLATDTTGD LILYLQPAEN RMVLNIADVA HPPIELMQLG
     DPLFVNPSFP PVAIGTYEDF IVNYVGNTVS ISNWRDNRDS VSFPTNSQVR SVCWASAGRI
     IVSGHEDGTV RVHHPFSNAY EEAVVERTVT NPAIDSGQRY LACLNSDKKL GLLDLRSYEW
     VTQDLCTTTG LVQSLKFNSD SEWIMVDDES GLFVVNCRDG KRKVELGNSK SASEFSADGT
     LVVTKADERV VELYDLQQMH SIDTVGLDLN SVLDTVRCDM DTLRYLLLSS EGKTQQLRVI
     DVSDGRIINE ISIKTSISGK GIYGRFIEKG HVSVVSDRNL FCDLSSENRV LVEGVPTPDF
     RHALALQLNP NSDTIEIQCR SVDDTDSLTS RPLKRAIDQF VIVSPKSDRV LVCSDNGQTK
     TLEVFTVGSL SLIDERFCDS MDEVEWTDDG ENIWIRGDDG LLSIWNPSSK TFRSYDFGDC
     KHSFMLTAGK KFISVKTDSI RIFDVDWLKL TNVTQFDAWS GVHVDELMNV QLLDGPWQSN
     SRLPSVKGVF VSIDPDSLES AVAATTAKLM WELGDRNFDI SLMTQAAQLK DRSHAGGGSD
     SWRWWGTIAN RLFEEQRYAD SLDASLNVLV SLGKEKEESD NYVVTLANIA KCQSKLGEFQ
     KARTCLTNAL AARDSIGWTD LRVQLLFELA TIDADAGQPE EFFENAEAFL EKTAPRKLEL
     WSSYSTLSIR LAREYRLKGR HDKAVVVVGK ILDDVKSGAG GLSDKKLLEI LLCLHAGKDF
     ANLIDVYQSF SYQPDSSEQI FYLGVGEILY AHAKILEGDG KDAFRITASA IKRMLSGTRN
     QEVLSQVEMQ LVKNAIEFIS KQSYENRKLR AISDALELY
//