ID J6H3L6_9FIRM Unreviewed; 642 AA.
AC J6H3L6; V9HUT9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Serine/threonine-protein kinase PrkC family protein {ECO:0000313|EMBL:EJU19970.1};
GN ORFNames=HMPREF1143_1647 {ECO:0000313|EMBL:EJU19970.1},
GN HMPREF9630_01378 {ECO:0000313|EMBL:EHL17853.1};
OS Peptoanaerobacter stomatis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoanaerobacter.
OX NCBI_TaxID=796937 {ECO:0000313|EMBL:EJU19970.1, ECO:0000313|Proteomes:UP000005244};
RN [1] {ECO:0000313|EMBL:EHL17853.1, ECO:0000313|Proteomes:UP000017818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM2 {ECO:0000313|EMBL:EHL17853.1,
RC ECO:0000313|Proteomes:UP000017818};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Eubacteriaceae bacterium CM2.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EJU19970.1, ECO:0000313|Proteomes:UP000005244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC8 {ECO:0000313|EMBL:EJU19970.1,
RC ECO:0000313|Proteomes:UP000005244};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJU19970.1}.
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DR EMBL; AFZF02000016; EHL17853.1; -; Genomic_DNA.
DR EMBL; ALNK01000037; EJU19970.1; -; Genomic_DNA.
DR RefSeq; WP_009528100.1; NZ_JH815226.1.
DR AlphaFoldDB; J6H3L6; -.
DR PATRIC; fig|796939.3.peg.620; -.
DR HOGENOM; CLU_000288_135_2_9; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000005244; Unassembled WGS sequence.
DR Proteomes; UP000017818; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 3.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR43671:SF13; LD04361P; 1.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR Pfam; PF03793; PASTA; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EJU19970.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005244};
KW Transferase {ECO:0000313|EMBL:EJU19970.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..279
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 347..414
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 415..482
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 487..550
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 642 AA; 71999 MW; E31E85F35A1BFC79 CRC64;
MDKIILGNRY ELLEKIADGG MSTVYKAYCH TLNRIVAVKI LKSEFSKDEE FLIKFNNEAK
AAASLNHANI INIYDVCQED DIAYIVMEYV DGINLKQLIS KKGKFSEKEA LDILRQICLA
LRDAHKNKIV HRDIKPHNIM INKDNIVKVG DFGIAKATTS ATITTVGGVI GSVHYFSPEQ
ARGGYMDERS DIYSLGVVFY ELLTGKIPYD GDSPINVALK HLHENITIPE EYKDKISPSI
QNMLLKMTQK NMDKRYTSVD QIISDIDKIQ DGNSNINYFD RDDDFNTRII KLPKEEVNEG
INKNKSKVKK RRIKKLPVTI LGITVILVVM FAILLINGGN IFDAIHNTNT TIIPDIKGKT
IIEAQKDLEK SDLKLKIMSE KEDDTQKEGT ILEQNPESGV KMRKGEEVSV VVAKEPQNIV
IVPSVLDKEE KEAKSILEQA NLKPSVDYEF NDNVEKNHVI SQDPSSDVKA KIDDVVKLKV
SKGKEVKQEK IPSFIGMSLD YVESNIGNFK VGNVSYEEDT SKKEGIVLHQ NPKANTTHDV
GTEIDFVINK LSKTNNENNT SNVSDLQIPV SKTITLVLPQ KDNLLLSVLD KLDNAVVYTT
TISTAVNQNV DITLSAYLGQ TKVYDIYING EYYSTTGEIV FN
//