ID   PKNB_MYCTA              Reviewed;         626 AA.
AC   A5TY84;
DT   13-SEP-2023, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   04-NOV-2026, entry version 121.
DE   RecName: Full=Serine/threonine-protein kinase PknB;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:24816602};
GN   Name=pknB {ECO:0000312|EMBL:ABQ71734.1};
GN   OrderedLocusNames=MRA_0016 {ECO:0000312|EMBL:ABQ71734.1};
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1] {ECO:0000312|EMBL:ABQ71734.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND AUTOPHOSPHORYLATION.
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=24816602; DOI=10.1128/jb.01625-14;
RA   Gupta M., Sajid A., Sharma K., Ghosh S., Arora G., Singh R., Nagaraja V.,
RA   Tandon V., Singh Y.;
RT   "HupB, a nucleoid-associated protein of Mycobacterium tuberculosis, is
RT   modified by serine/threonine protein kinases in vivo.";
RL   J. Bacteriol. 196:2646-2657(2014).
CC   -!- FUNCTION: A serine/threonine-protein kinase, acts on HupB in vitro
CC       (PubMed:24816602). Protein kinase that regulates many aspects of
CC       mycobacterial physiology, and is critical for growth in vitro and
CC       survival of the pathogen in the host. Is a key component of a signal
CC       transduction pathway that regulates cell growth, cell shape and cell
CC       division. Also catalyzes the phosphorylation of the core proteasome
CC       alpha-subunit (PrcA), and thereby regulates the proteolytic activity of
CC       the proteasome. Is a major regulator of the oxygen-dependent
CC       replication switch since PknB activity is necessary for reactivation of
CC       cells from the hypoxic state (By similarity). Shows a strong preference
CC       for Thr versus Ser as the phosphoacceptor (Probable).
CC       {ECO:0000250|UniProtKB:P9WI81, ECO:0000269|PubMed:24816602,
CC       ECO:0000305|PubMed:24816602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:0000305|PubMed:24816602};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:24816602};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WI81}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WI81};
CC       Single-pass membrane protein {ECO:0000255}. Note=Localizes to septum
CC       and cell poles. {ECO:0000250|UniProtKB:P9WI81}.
CC   -!- INDUCTION: Transcribed at highest levels in early log-phase, decreases
CC       as cells grow older. {ECO:0000269|PubMed:24816602}.
CC   -!- PTM: Autophosphorylates. {ECO:0000269|PubMed:24816602}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CP000611; ABQ71734.1; -; Genomic_DNA.
DR   RefSeq; WP_003400356.1; NC_009525.1.
DR   AlphaFoldDB; A5TY84; -.
DR   SMR; A5TY84; -.
DR   GeneID; 45423973; -.
DR   KEGG; mra:MRA_0016; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2815; Bacteria.
DR   HOGENOM; CLU_000288_135_2_11; -.
DR   OMA; AAFQYYV; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   FunFam; 1.10.510.10:FF:000021; Serine/threonine protein kinase; 1.
DR   FunFam; 3.30.200.20:FF:000035; Serine/threonine protein kinase Stk1; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 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   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..626
FT                   /note="Serine/threonine-protein kinase PknB"
FT                   /id="PRO_0000458845"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          11..274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          356..422
FT                   /note="PASTA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          423..490
FT                   /note="PASTA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          491..557
FT                   /note="PASTA 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   DOMAIN          558..626
FT                   /note="PASTA 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT   REGION          299..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         17..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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
//