ID A0A417CAZ7_9FIRM Unreviewed; 633 AA.
AC A0A417CAZ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Stk1 family PASTA domain-containing Ser/Thr kinase {ECO:0000313|EMBL:RHS92896.1};
GN Name=pknB {ECO:0000313|EMBL:RHS92896.1};
GN ORFNames=DW911_07735 {ECO:0000313|EMBL:RHS92896.1};
OS Erysipelatoclostridium sp. AM42-17.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=2293102 {ECO:0000313|EMBL:RHS92896.1, ECO:0000313|Proteomes:UP000284957};
RN [1] {ECO:0000313|EMBL:RHS92896.1, ECO:0000313|Proteomes:UP000284957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM42-17 {ECO:0000313|EMBL:RHS92896.1,
RC ECO:0000313|Proteomes:UP000284957};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHS92896.1}.
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DR EMBL; QUIN01000018; RHS92896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417CAZ7; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000284957; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 4.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.10.20; -; 4.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51178; PASTA; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:RHS92896.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000284957};
KW Transferase {ECO:0000313|EMBL:RHS92896.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 356..424
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 425..491
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 495..559
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 560..632
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 633 AA; 70152 MW; 0FE8736D5A189B10 CRC64;
MNKIIADRYE IIDLIGQGGM ADVYLAKDTI LNRAIAIKIL RTSLAKDPVY ITRFQREASA
AAALSDKNIV EIYDVGEEGN QYYIVMEYVP GTTLKELILK RGALHMVEAV DIMKQVVSGV
AKAHQLGIIH RDLKPQNILV TDTGTAKIAD FGIASIQSLT HVTQTDVIMG SLHYLAPELA
RGEKATAQSD IYALGIVFYE LLRGEVPFNG ESPVNIALKH MQEDLPSLRE FNPSILQSVE
NIIIKATAKN LNDRYHSAKE MLADLQTCLS RKNEEKLEFY HDINDEPTIV VGQNEIFDQE
EPEHLQREKS EDKKNKKKKS LLQRIKEKDL KVIIPLAAGI IAVLCLLMYF ILFAGGNDNT
VMPDLTGYTK EKAQKILSEY DVKISDTVYK ELSDKYTKGK IIATNPKSGT TINKGDTVTL
TVSKGKYIVV GNYIGMTYDE AKIKLKKHFN VEKEEAVSSQ KAGTVIGQSL KSGYKQDPTE
KDRTIVLTVS KGQYTVLDDY TGMTYDGAKA KLEALGFVVS RRDEVSDETA GTVIDQNLAV
GYRVDPSDKN RHITLTVSSG YSQTVPSVNG LSYSDAKSNL ENLGFVVTLS PTQFPDDGSV
DETMKGKVYK QSVSAGTKVD KKGTTITIYY YQE
//
