ID A0A0E8V2H6_MYCTX Unreviewed; 626 AA.
AC A0A0E8V2H6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Serine/threonine-protein kinase PknB {ECO:0000256|ARBA:ARBA00014672};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=pknB {ECO:0000313|EMBL:COW15035.1};
GN ORFNames=A4S10_00020 {ECO:0000313|EMBL:OMH57873.1}, ERS007665_00437
GN {ECO:0000313|EMBL:CNU11649.1}, ERS007679_02785
GN {ECO:0000313|EMBL:COV95958.1}, ERS007688_02189
GN {ECO:0000313|EMBL:CFE52970.1}, ERS007703_02893
GN {ECO:0000313|EMBL:COW15035.1}, ERS007720_01005
GN {ECO:0000313|EMBL:COV83007.1}, ERS027646_01287
GN {ECO:0000313|EMBL:CKS11483.1}, ERS027659_02355
GN {ECO:0000313|EMBL:CKR89653.1}, ERS027661_01535
GN {ECO:0000313|EMBL:CKR52561.1}, ERS053720_03032
GN {ECO:0000313|EMBL:CFH90588.1}, GJE03_00090
GN {ECO:0000313|EMBL:QGK77352.1}, SAMEA2683035_00154
GN {ECO:0000313|EMBL:SGH03542.1};
OS Mycobacterium tuberculosis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773 {ECO:0000313|EMBL:COW15035.1, ECO:0000313|Proteomes:UP000038802};
RN [1] {ECO:0000313|Proteomes:UP000038802, ECO:0000313|Proteomes:UP000044938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2926STDY5723788 {ECO:0000313|EMBL:SGH03542.1,
RC ECO:0000313|Proteomes:UP000182946}, Bir 172
RC {ECO:0000313|EMBL:CKS11483.1, ECO:0000313|Proteomes:UP000048948}, Bir
RC 185 {ECO:0000313|EMBL:CKR89653.1, ECO:0000313|Proteomes:UP000050164},
RC Bir 187 {ECO:0000313|EMBL:CKR52561.1,
RC ECO:0000313|Proteomes:UP000049023}, D00700688
RC {ECO:0000313|EMBL:CNU11649.1, ECO:0000313|Proteomes:UP000045274},
RC G09801536 {ECO:0000313|EMBL:COV95958.1,
RC ECO:0000313|Proteomes:UP000045842}, H09601792
RC {ECO:0000313|EMBL:CFE52970.1, ECO:0000313|Proteomes:UP000046947},
RC K00500041 {ECO:0000313|Proteomes:UP000038802}, and M09401471
RC {ECO:0000313|EMBL:COV83007.1, ECO:0000313|Proteomes:UP000044938};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:COW15035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K00500041 {ECO:0000313|EMBL:COW15035.1};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CFH90588.1, ECO:0000313|Proteomes:UP000046674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0351H {ECO:0000313|EMBL:CFH90588.1,
RC ECO:0000313|Proteomes:UP000046674};
RG Pathogen Informatics;
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:OMH57873.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH57873.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M., Bigi F., Soria M.A.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:OMH57873.1, ECO:0000313|Proteomes:UP000189452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6548 {ECO:0000313|EMBL:OMH57873.1,
RC ECO:0000313|Proteomes:UP000189452};
RA Bigi M.M., Lopez B., Blanco F.C., Sasiain M.C., De La Barrera S.,
RA Ritacco V., Bigi F., Soria M.A.;
RT "Protein polymorphisms may explain contrasting epidemiological fitness of
RT two variants of a multidrug-resistant Mycobacterium tuberculosis strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:QGK77352.1, ECO:0000313|Proteomes:UP000388593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUSMDU00018547 {ECO:0000313|EMBL:QGK77352.1,
RC ECO:0000313|Proteomes:UP000388593};
RA Baines S.L., Goncalves da Silva A., Carter G.P., Jennison A.V.,
RA Rathnayake I.U., Graham R.M.A., Sintchenko V., Wang Q., Rockett R.J.,
RA Timms V.J., Martinez E., Ballard S., Tomita T., Isles N., Horan K.A.,
RA Pitchers W., Stinear T.P., Williamson D.A., Howden B.P., Seemann T.;
RT "Complete microbial genomes for public health in Australia and Southwest
RT Pacific.";
RL Submitted (NOV-2019) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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DR EMBL; CFOH01000342; CFE52970.1; -; Genomic_DNA.
DR EMBL; CFSW01000021; CFH90588.1; -; Genomic_DNA.
DR EMBL; CNFU01000268; CKR52561.1; -; Genomic_DNA.
DR EMBL; CNFT01000547; CKR89653.1; -; Genomic_DNA.
DR EMBL; CNGE01000179; CKS11483.1; -; Genomic_DNA.
DR EMBL; CQPW01000048; CNU11649.1; -; Genomic_DNA.
DR EMBL; CSAJ01000089; COV83007.1; -; Genomic_DNA.
DR EMBL; CSAD01000422; COV95958.1; -; Genomic_DNA.
DR EMBL; CSAE01000350; COW15035.1; -; Genomic_DNA.
DR EMBL; LWDQ01000001; OMH57873.1; -; Genomic_DNA.
DR EMBL; CP045962; QGK77352.1; -; Genomic_DNA.
DR EMBL; FPTZ01000001; SGH03542.1; -; Genomic_DNA.
DR RefSeq; WP_003400356.1; NZ_WFKY01000012.1.
DR STRING; 115862.BBG46_00230; -.
DR GeneID; 45423973; -.
DR PATRIC; fig|1773.206.peg.326; -.
DR OMA; DPDYRYQ; -.
DR Proteomes; UP000038802; Unassembled WGS sequence.
DR Proteomes; UP000044938; Unassembled WGS sequence.
DR Proteomes; UP000045274; Unassembled WGS sequence.
DR Proteomes; UP000045842; Unassembled WGS sequence.
DR Proteomes; UP000046674; Unassembled WGS sequence.
DR Proteomes; UP000046947; Unassembled WGS sequence.
DR Proteomes; UP000048948; Unassembled WGS sequence.
DR Proteomes; UP000049023; Unassembled WGS sequence.
DR Proteomes; UP000050164; Unassembled WGS sequence.
DR Proteomes; UP000182946; Unassembled WGS sequence.
DR Proteomes; UP000189452; Chromosome.
DR Proteomes; UP000388593; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR Pfam; PF03793; PASTA; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00740; PASTA; 4.
DR SMART; SM00220; S_TKc; 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:COW15035.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:COW15035.1};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:SGH03542.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..274
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 356..422
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 423..490
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 491..557
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT DOMAIN 558..626
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 299..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 626 AA; 66510 MW; 6C27EEBE9D5A453B CRC64;
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA
QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL RDIVHTEGPM TPKRAIEVIA
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSGNSV TQTAAVIGTA
QYLSPEQARG DSVDARSDVY SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH
EGLSADLDAV VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI NTFGGITRDV
QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI GTDPAANTSV SAGDEITVNV
STGPEQREIP DVSTLTYAEA VKKLTAAGFG RFKQANSPST PELVGKVIGT NPPANQTSAI
TNVVIIIVGS GPATKDIPDV AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP
AGTTVPVDSV IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH
NRVVYQNPPA GTGVNRDGII TLRFGQ
//