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PKNI_MYCTO
ID   PKNI_MYCTO              Reviewed;         585 AA.
AC   P9WI68; L0TB90; P65730; Q10964;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Serine/threonine-protein kinase PknI;
DE            EC=2.7.11.1;
GN   Name=pknI; OrderedLocusNames=MT2982;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Plays an important role in slowing down the growth of
CC       mycobacteria within the infected host. {ECO:0000250}.
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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated at serine and threonine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47308.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70747; B70747.
DR   RefSeq; WP_003900593.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WI68; -.
DR   SMR; P9WI68; -.
DR   EnsemblBacteria; AAK47308; AAK47308; MT2982.
DR   GeneID; 45426901; -.
DR   KEGG; mtc:MT2982; -.
DR   PATRIC; fig|83331.31.peg.3222; -.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Serine/threonine-protein kinase; Transferase;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..585
FT                   /note="Serine/threonine-protein kinase PknI"
FT                   /id="PRO_0000428059"
FT   TOPO_DOM        1..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..585
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          12..252
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          546..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         18..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   585 AA;  61805 MW;  E52EACFF4A69C3EC CRC64;
     MALASGVTFA GYTVVRMLGC SAMGEVYLVQ HPGFPGWQAL KVLSPAMAAD DEFRRRFQRE
     TEVAARLFHP HILEVHDRGE FDGQLWIAMD YVDGIDATQH MADRFPAVLP VGEVLAIVTA
     VAGALDYAHQ RGLLHRDVNP ANVVLTSQSA GDQRILLADF GIASQPSYPA PELSAGADVD
     GRADQYALAL TAIHLFAGAP PVDRSHTGPL QPPKLSAFRP DLARLDGVLS RALATAPADR
     FGSCREFADA MNEQAGVAIA DQSSGGVDAS EVTAAAGEEA YVVDYPAYGW PEAVDCKEPS
     ARAPAPAAPT PQRRGSMLQS AAGVLARRLD NFSTATKAPA SPTRRRPRRI LVGAVAVLLL
     AGLFAVGIVI GRKTNTTATE VARPPTSGSA VPSAPTTTVA VTAPVPLDGT YRIEIQRSKQ
     TYDYTPTPQP PDVNTWWAFR TSCTPTECLA AATMLDDNDH TQAKTPPVRP FLMQFGEGQW
     KSRPETVQFP CVGPNGSPST QATTQLLALR PQPQGDLVGE MVVTVHSNEC GQQGAVIRIP
     AVASRSGDLP PAVTVPDPAT IPDTPDTTST ATLTPPTTTA PGPGR
 
 
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