Serine/threonine-protein kinase PknB - Mycobacterium tuberculosis

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P0A5S4 (PKNB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PknB
EC=2.7.11.1

Gene names

Name:	pknB
Ordered Locus Names:	Rv0014c, MT0017
ORF Names:	MTCY10H4.14c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as GarA, GlmU, PapA5, PbpA, FhaB (Rv0019c), FhaA (Rv0020c), MviN, PstP, EmbR, Rv1422 and Rv1747. Shows a strong preference for Thr versus Ser as the phosphoacceptor. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.12 Ref.20
Enzyme regulation	Interaction of the PASTA domains with peptidoglycan leads to septal and polar localization of PknB, and dimerization of the intracellular kinase domain. Dimerization activates the kinase domain via an allosteric mechanism, triggering autophosphorylation and phosphorylation of target proteins. Inhibited by mitoxantrone. Inhibition prevents mycobacterial growth. Ref.14 Ref.16 Ref.21 Ref.23
Subunit structure	Homodimer. Interacts with the FHA domain of GarA, FhaB and FhaA. Ref.7 Ref.12 Ref.14 Ref.17 Ref.21
Subcellular location	Cell membrane; Single-pass membrane protein. Note: Localizes to septum and cell poles. Ref.16
Induction	Expressed predominantly in exponential phase. Ref.6 Ref.14 Ref.16 Ref.21 Ref.23
Domain	The PASTA domains interact with peptidoglycans and are required for PknB localization. Ref.16
Post-translational modification	Autophosphorylated. Dephosphorylated by PstP. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.20 Ref.22
Disruption phenotype	Essential for growth, it cannot be disrupted. Ref.10
Miscellaneous	Overexpression causes major growth and morphological changes that indicate defects in cell wall synthesis and possibly in cell division (Ref.6).
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 4 PASTA domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	growth Inferred from mutant phenotype PubMed 12657046 Ref.6 Ref.10. Source: MTBBASE negative regulation of catalytic activity Inferred from direct assay PubMed 16873379. Source: MTBBASE negative regulation of fatty acid biosynthetic process Inferred from direct assay PubMed 20178986. Source: MTBBASE negative regulation of protein binding Inferred from direct assay PubMed 18685700. Source: MTBBASE positive regulation of DNA binding Inferred from direct assay Ref.9. Source: MTBBASE positive regulation of catalytic activity Inferred from direct assay PubMed 16873379. Source: MTBBASE protein autophosphorylation Inferred from direct assay Ref.4 Ref.6. Source: MTBBASE regulation of cell shape Inferred from mutant phenotype Ref.6. Source: MTBBASE regulation of transferase activity Inferred from direct assay Ref.13. Source: MTBBASE response to host immune response Inferred from direct assay Ref.4. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from direct assay Ref.4. Source: MTBBASE penicillin binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from direct assay Ref.4 Ref.6 PubMed 18685700 Ref.13 Ref.12. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

Serine/threonine-protein kinase PknB

PRO_0000171208

Regions

Topological domain

1 – 332

332

Cytoplasmic Potential

Transmembrane

333 – 353

Helical; Potential

Topological domain

354 – 626

273

Extracellular Potential

Domain

11 – 274

264

Protein kinase

Domain

356 – 422

PASTA 1

Domain

423 – 490

PASTA 2

Domain

491 – 557

PASTA 3

Domain

558 – 626

PASTA 4

Nucleotide binding

17 – 25

ATP

Nucleotide binding

93 – 95

ATP

Nucleotide binding

140 – 143

ATP

Sites

Active site

138

Proton acceptor

Metal binding

143

Magnesium

Metal binding

156

Magnesium

Binding site

ATP

Binding site

156

ATP

Amino acid modifications

Modified residue

166

Phosphoserine; by autocatalysis Ref.5 Ref.20

Modified residue

169

Phosphoserine; by autocatalysis Ref.20

Modified residue

171

Phosphothreonine; by autocatalysis Ref.3 Ref.5 Ref.6 Ref.20 Ref.22

Modified residue

173

Phosphothreonine; by autocatalysis Ref.3 Ref.5 Ref.6 Ref.20

Modified residue

294

Phosphothreonine; by autocatalysis Ref.5 Ref.20

Modified residue

295

Phosphoserine; by autocatalysis Ref.20

Modified residue

309

Phosphothreonine; by autocatalysis Ref.5

Experimental info

Mutagenesis

R → A: Impairs kinase activity. Ref.14

Mutagenesis

L → D: Impairs kinase activity. Ref.14

Mutagenesis

K → M: Lack of autophosphorylation. Decreases affinity for FhaB. Ref.6 Ref.12

Mutagenesis

D → A: Impairs kinase activity. Ref.14

Mutagenesis

138

D → N: Impairs kinase activity. Ref.14

Mutagenesis

171

T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. Ref.3 Ref.7 Ref.12

Mutagenesis

173

T → A: Reduces activity and autophosphorylation. Decreases interaction with GarA. Ref.3 Ref.7 Ref.12

Mutagenesis

294

T → A: Does not affect activity. Ref.12

Mutagenesis

309

T → A: Does not affect activity. Ref.12

Secondary structure

626

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A5S4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 6C27EEBE9D5A453B
Show »

FASTA

626

66,510

        10         20         30         40         50         60 
MTTPSHLSDR YELGEILGFG GMSEVHLARD LRLHRDVAVK VLRADLARDP SFYLRFRREA 

        70         80         90        100        110        120 
QNAAALNHPA IVAVYDTGEA ETPAGPLPYI VMEYVDGVTL RDIVHTEGPM TPKRAIEVIA 

       130        140        150        160        170        180 
DACQALNFSH QNGIIHRDVK PANIMISATN AVKVMDFGIA RAIADSGNSV TQTAAVIGTA 

       190        200        210        220        230        240 
QYLSPEQARG DSVDARSDVY SLGCVLYEVL TGEPPFTGDS PVSVAYQHVR EDPIPPSARH 

       250        260        270        280        290        300 
EGLSADLDAV VLKALAKNPE NRYQTAAEMR ADLVRVHNGE PPEAPKVLTD AERTSLLSSA 

       310        320        330        340        350        360 
AGNLSGPRTD PLPRQDLDDT DRDRSIGSVG RWVAVVAVLA VLTVVVTIAI NTFGGITRDV 

       370        380        390        400        410        420 
QVPDVRGQSS ADAIATLQNR GFKIRTLQKP DSTIPPDHVI GTDPAANTSV SAGDEITVNV 

       430        440        450        460        470        480 
STGPEQREIP DVSTLTYAEA VKKLTAAGFG RFKQANSPST PELVGKVIGT NPPANQTSAI 

       490        500        510        520        530        540 
TNVVIIIVGS GPATKDIPDV AGQTVDVAQK NLNVYGFTKF SQASVDSPRP AGEVTGTNPP 

       550        560        570        580        590        600 
AGTTVPVDSV IELQVSKGNQ FVMPDLSGMF WVDAEPRLRA LGWTGMLDKG ADVDAGGSQH 

       610        620 
NRVVYQNPPA GTGVNRDGII TLRFGQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis." Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T., Cervenansky C., Alzari P.M. Mol. Microbiol. 49:1493-1508(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 162-189, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-171 AND THR-173, MUTAGENESIS OF THR-171 AND THR-173, MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.
[4]	"Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB." Av-Gay Y., Jamil S., Drews S.J. Infect. Immun. 67:5676-5682(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION. Strain: ATCC 25618 / H37Rv.
[5]	"Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases." Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P., Boitel B., Cole S.T., Alzari P.M., Cervenansky C. Biochem. Biophys. Res. Commun. 333:858-867(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-166; THR-171; THR-173; THR-294 AND THR-309, MASS SPECTROMETRY.
[6]	"The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape." Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C., Husson R.N. Genes Dev. 19:1692-1704(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, PHOSPHORYLATION AT THR-171 AND THR-173, OVEREXPRESSION, MUTAGENESIS OF LYS-40. Strain: ATCC 25618 / H37Rv.
[7]	"Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions." Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cervenansky C., Alzari P.M. J. Mol. Biol. 350:953-963(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GARA, MUTAGENESIS OF THR-171 AND THR-173. Strain: ATCC 25618 / H37Rv.
[8]	"Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains." Grundner C., Gay L.M., Alber T. Protein Sci. 14:1918-1921(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]	"EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis." Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y. FEBS J. 273:2711-2721(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, DEPHOSPHORYLATION BY PSTP.
[10]	"The Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growth." Fernandez P., Saint-Joanis B., Barilone N., Jackson M., Gicquel B., Cole S.T., Alzari P.M. J. Bacteriol. 188:7778-7784(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: ATCC 25618 / H37Rv.
[11]	"The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division." Dasgupta A., Datta P., Kundu M., Basu J. Microbiology 152:493-504(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH PBPA AS SUBSTRATE. Strain: ATCC 25618 / H37Rv.
[12]	"Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis." Gupta M., Sajid A., Arora G., Tandon V., Singh Y. J. Biol. Chem. 284:34723-34734(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FHAB, MUTAGENESIS OF LYS-40; THR-171; THR-173; THR-294 AND THR-309.
[13]	"PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity." Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K. J. Mol. Biol. 386:451-464(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH GLMU AS SUBSTRATE.
[14]	"Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB." Lombana T.N., Echols N., Good M.C., Thomsen N.D., Ng H.L., Greenstein A.E., Falick A.M., King D.S., Alber T. Structure 18:1667-1677(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ARG-10; LEU-33; ASP-76 AND ASP-138. Strain: ATCC 25618 / H37Rv.
[15]	"Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB." Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y. PLoS ONE 6:E17871-E17871(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A KINASE WITH PSTP AS SUBSTRATE. Strain: ATCC 25618 / H37Rv.
[16]	"The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization." Mir M., Asong J., Li X., Cardot J., Boons G.J., Husson R.N. PLoS Pathog. 7:E1002182-E1002182(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN.
[17]	"Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase." Roumestand C., Leiba J., Galophe N., Margeat E., Padilla A., Bessin Y., Barthe P., Molle V., Cohen-Gonsaud M. Structure 19:1525-1534(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FHAA. Strain: ATCC 25618 / H37Rv.
[18]	"A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria." Gee C.L., Papavinasasundaram K.G., Blair S.R., Baer C.E., Falick A.M., King D.S., Griffin J.E., Venghatakrishnan H., Zukauskas A., Wei J.R., Dhiman R.K., Crick D.C., Rubin E.J., Sassetti C.M., Alber T. Sci. Signal. 5:RA7-RA7(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis." Ortiz-Lombardia M., Pompeo F., Boitel B., Alzari P.M. J. Biol. Chem. 278:13094-13100(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-279 IN COMPLEX WITH ATP.
[20]	"Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases." Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., Alber T. Nat. Struct. Biol. 10:168-174(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-308 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY, METAL BINDING AT ASN-143 AND ASP-156, ATP BINDING AT LYS-40, PHOSPHORYLATION AT SER-166; SER-169; THR-171; THR-173; THR-294 AND SER-295, MASS SPECTROMETRY.
[21]	"The structure of PknB in complex with mitoxantrone, an ATP-competitive inhibitor, suggests a mode of protein kinase regulation in mycobacteria." Wehenkel A., Fernandez P., Bellinzoni M., Catherinot V., Barilone N., Labesse G., Jackson M., Alzari P.M. FEBS Lett. 580:3018-3022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 1-279 IN COMPLEX WITH MITOXANTRONE, ENZYME REGULATION, SUBUNIT.
[22]	"Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase." Mieczkowski C., Iavarone A.T., Alber T. EMBO J. 27:3186-3197(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-308 IN COMPLEX WITH ADP, PHOSPHORYLATION AT THR-171.
[23]	"The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation." Barthe P., Mukamolova G.V., Roumestand C., Cohen-Gonsaud M. Structure 18:606-615(2010) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 355-491, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000516 Genomic DNA. Translation: AAK44239.1.
AL123456 Genomic DNA. Translation: CCP42736.1.

PIR

D70699.

RefSeq

NP_214528.1. NC_000962.3.
NP_334425.1. NC_002755.2.
YP_006513328.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MRU	X-ray	3.00	A/B	1-308	[»]
1O6Y	X-ray	2.20	A	1-279	[»]
2FUM	X-ray	2.89	A/B/C/D	1-279	[»]
2KUD	NMR	-	A	355-491	[»]
2KUE	NMR	-	A	423-557	[»]
2KUF	NMR	-	A	491-626	[»]
2KUI	NMR	-	A	355-626	[»]
3F61	X-ray	1.80	A	1-308	[»]
3F69	X-ray	2.80	A/B	1-308	[»]

ProteinModelPortal

P0A5S4.

SMR

P0A5S4. Positions 2-287, 355-626.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-13376N.

IntAct

P0A5S4. 3 interactions.

MINT

MINT-7293801.

STRING

83332.Rv0014c.

PTM databases

PhosSite

P0603150.

Proteomic databases

PRIDE

P0A5S4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK44239; AAK44239; MT0017.

GeneID

13315991.
887072.
922465.

KEGG

mtc:MT0017.
mtu:Rv0014c.

PATRIC

18121764. VBIMycTub22151_0018.

Organism-specific databases

TubercuList

Rv0014c.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000037185.

K08884.

OMA

TGKDPGT.

ProtClustDB

CLSK790192.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR005543. PASTA.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF03793. PASTA. 4 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00740. PASTA. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51178. PASTA. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A5S4.

ChEMBL

CHEMBL1908385.

EvolutionaryTrace

P0A5S4.

Entry information

Entry name

PKNB_MYCTU

Accession

Primary (citable) accession number: P0A5S4
Secondary accession number(s): L0T5F6, P71584

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents