ID   Q7UT84_RHOBA            Unreviewed;       555 AA.
AC   Q7UT84;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=ppkA {ECO:0000313|EMBL:CAD73553.1};
GN   OrderedLocusNames=RB4031 {ECO:0000313|EMBL:CAD73553.1};
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD73553.1, ECO:0000313|Proteomes:UP000001025};
RN   [1] {ECO:0000313|EMBL:CAD73553.1, 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; BX294139; CAD73553.1; -; Genomic_DNA.
DR   RefSeq; NP_865868.1; NC_005027.1.
DR   RefSeq; WP_011119689.1; NC_005027.1.
DR   AlphaFoldDB; Q7UT84; -.
DR   STRING; 243090.RB4031; -.
DR   EnsemblBacteria; CAD73553; CAD73553; RB4031.
DR   KEGG; rba:RB4031; -.
DR   PATRIC; fig|243090.15.peg.1881; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_033241_0_0_0; -.
DR   InParanoid; Q7UT84; -.
DR   OrthoDB; 6111975at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CAD73553.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAD73553.1};
KW   Transferase {ECO:0000313|EMBL:CAD73553.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        514..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..351
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   555 AA;  61390 MW;  4A17D3D0494468C0 CRC64;
     MNDPDSPSSL DSVLAEILVR EENGERPDPH EYLEKHPDHA EELRDFFRNH RWLGSEDAEP
     ATLVGQTIGE FRIIREVARG GMGVVYEAQQ DSLRRVVAIK LIGDGVLAND EVRLRFRVEA
     EAAASLSHPN ILPIHSIGCW RGIDYFVMPM VSGDSLQSLV DQQREGCRDG SMATAEVKEC
     VMKAVAFMRD ISRGVAYAHS RGIIHRDLKP ENVLIDDGVP KIVDFGLAKF HRDAPELTRN
     GQVLGTPHYM SPEQARGCGD LTDAVDVYAL GGMLFSMLTG SPPHSGESTA EVLSRVLSDE
     PPSLRLAYPG GMPRLPELAD LDHVIQRAMA CEPTERYRSA DELADDLDRI LVGETPLAAP
     DGLVHRMSRE LARDQHLHAF QNWGRALRGI GYVVLAAHIA MFVIMQWVYV DTPSDLAAWS
     QPAFWGYFVP RLLMLAGIAW VIGRARDGLW LPRISAERPV WSIWLGYLVA LSSINLLWIS
     GNLDHSGVMV MACVMSGFAF IAIAGHMWGG SALLGMGFIG MAFASVAIPV AAPLFLGGWW
     MVTMLVFSKR YRRME
//