ACR_MYCTU
ID ACR_MYCTU Reviewed; 144 AA.
AC P9WMK1; L0TBA7; P0A5B7; P30223;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Alpha-crystallin;
DE Short=Acr;
DE AltName: Full=14 kDa antigen;
DE AltName: Full=16 kDa antigen;
DE AltName: Full=HSP 16.3;
DE AltName: Full=Nox16;
GN Name=hspX; Synonyms=acr; OrderedLocusNames=Rv2031c; ORFNames=MTV018.18c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=1370952; DOI=10.1128/jb.174.4.1352-1359.1992;
RA Verbon A., Hartskeerl R.A., Schuitema A., Kolk A.H.J., Young D.B.,
RA Lathigra R.;
RT "The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is
RT related to the alpha-crystallin family of low-molecular-weight heat shock
RT proteins.";
RL J. Bacteriol. 174:1352-1359(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-144, CHARACTERIZATION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=1563797; DOI=10.1128/iai.60.5.2066-2074.1992;
RA Lee B.-Y., Hefta S.A., Brennan P.J.;
RT "Characterization of the major membrane protein of virulent Mycobacterium
RT tuberculosis.";
RL Infect. Immun. 60:2066-2074(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-13, AND INDUCTION BY NITRIC OXIDE (NO).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9864257; DOI=10.1128/iai.67.1.460-465.1999;
RA Garbe T.R., Hibler N.S., Deretic V.;
RT "Response to reactive nitrogen intermediates in Mycobacterium tuberculosis:
RT induction of the 16-kilodalton alpha-crystallin homolog by exposure to
RT nitric oxide donors.";
RL Infect. Immun. 67:460-465(1999).
RN [5]
RP FUNCTION AS A CHAPERONE, INDUCTION IN STATIONARY PHASE, AND INDUCTION BY
RP HYPOXIA.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=8755875; DOI=10.1128/jb.178.15.4484-4492.1996;
RA Yuan Y., Crane D.D., Barry C.E. III;
RT "Stationary phase-associated protein expression in Mycobacterium
RT tuberculosis: function of the mycobacterial alpha-crystallin homolog.";
RL J. Bacteriol. 178:4484-4492(1996).
RN [6]
RP INDUCTION BY HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11416222; DOI=10.1073/pnas.121172498;
RA Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I.,
RA Schoolnik G.K.;
RT "Regulation of the Mycobacterium tuberculosis hypoxic response gene
RT encoding alpha -crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7534-7539(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, MULTIPLE FORMS, AND INDUCTION BY
RP HYPOXIA.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12057942; DOI=10.1128/jb.184.13.3485-3491.2002;
RA Rosenkrands I., Slayden R.A., Crawford J., Aagaard C., Barry C.E. III,
RA Andersen P.;
RT "Hypoxic response of Mycobacterium tuberculosis studied by metabolic
RT labeling and proteome analysis of cellular and extracellular proteins.";
RL J. Bacteriol. 184:3485-3491(2002).
RN [8]
RP INDUCTION BY NITRIC OXIDE (NO); BY HYPOXIA; IN MOUSE MODEL AND DORMANCY
RP REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12953092; DOI=10.1084/jem.20030205;
RA Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA Sherman D.R., Schoolnik G.K.;
RT "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT tuberculosis dormancy program.";
RL J. Exp. Med. 198:705-713(2003).
RN [9]
RP INDUCTION BY HOST IMMUNITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12506197; DOI=10.1073/pnas.0136863100;
RA Shi L., Jung Y.J., Tyagi S., Gennaro M.L., North R.J.;
RT "Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium
RT tuberculosis transcription pattern characteristic of nonreplicating
RT persistence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:241-246(2003).
RN [10]
RP INDUCTION BY ANAEROBISIS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=S-02293 Harlingen;
RX PubMed=15528667; DOI=10.1099/mic.0.27284-0;
RA Starck J., Kallenius G., Marklund B.I., Andersson D.I., Akerlund T.;
RT "Comparative proteome analysis of Mycobacterium tuberculosis grown under
RT aerobic and anaerobic conditions.";
RL Microbiology 150:3821-3829(2004).
RN [11]
RP DISRUPTION PHENOTYPE, AND PROBABLE OPERON STRUCTURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16428728; DOI=10.1128/iai.74.2.861-868.2006;
RA Hu Y., Movahedzadeh F., Stoker N.G., Coates A.R.;
RT "Deletion of the Mycobacterium tuberculosis alpha-crystallin-like hspX gene
RT causes increased bacterial growth in vivo.";
RL Infect. Immun. 74:861-868(2006).
RN [12]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17145953; DOI=10.1128/iai.01137-06;
RA Roupie V., Romano M., Zhang L., Korf H., Lin M.Y., Franken K.L.,
RA Ottenhoff T.H., Klein M.R., Huygen K.;
RT "Immunogenicity of eight dormancy regulon-encoded proteins of Mycobacterium
RT tuberculosis in DNA-vaccinated and tuberculosis-infected mice.";
RL Infect. Immun. 75:941-949(2007).
RN [13]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17609369; DOI=10.1073/pnas.0705054104;
RA Kumar A., Toledo J.C., Patel R.P., Lancaster J.R. Jr., Steyn A.J.;
RT "Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia
RT sensor.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11568-11573(2007).
RN [14]
RP INDUCTION BY CARBON MONOXIDE (CO).
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA Shiloh M.U., Manzanillo P., Cox J.S.;
RT "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT macrophage infection.";
RL Cell Host Microbe 3:323-330(2008).
RN [15]
RP INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA Agarwal A., Steyn A.J.;
RT "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT tuberculosis dormancy regulon.";
RL J. Biol. Chem. 283:18032-18039(2008).
RN [16]
RP PUPYLATION AT LYS-64; LYS-85; LYS-114 AND LYS-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Acts as a chaperone, as it has a significant ability to
CC suppress the thermal denaturation of alcohol dehydrogenase. Cells
CC overexpressing this gene grow more slowly than wild-type cells, and are
CC less susceptible to autolysis following saturation of the culture in
CC vitro, suggesting this protein may slow down the growth rate of
CC M.tuberculosis in culture and by extension during macrophage infection.
CC {ECO:0000269|PubMed:8755875}.
CC -!- INTERACTION:
CC P9WMK1; P9WI75: pknF; NbExp=2; IntAct=EBI-2945921, EBI-2945875;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1563797}. Secreted,
CC cell wall {ECO:0000269|PubMed:1563797}. Note=Probably the external side
CC of the cell wall; the protein is very abundant in older organisms and
CC surface coating could be the result of autolysis of older organisms.
CC -!- INDUCTION: Induced by several reactive nitrogen intermediates including
CC S-nitroso glutathione (at protein level). Induced in stationary phase
CC (at protein level). A member of the dormancy regulon. Induced in
CC response to reduced oxygen tension (hypoxia) (at protein level), low
CC levels of nitric oxide (NO) and carbon monoxide (CO). It is hoped that
CC this regulon will give insight into the latent, or dormant phase of
CC infection. Induced in mouse lungs at the same time that adaptive host
CC immunity induces bacterial growth arrest; induction is dependent on
CC interferon gamma. A member of the probable hspX-Rv2030c-pfkB-Rv2028c
CC operon. {ECO:0000269|PubMed:11416222, ECO:0000269|PubMed:12057942,
CC ECO:0000269|PubMed:12506197, ECO:0000269|PubMed:12953092,
CC ECO:0000269|PubMed:15528667, ECO:0000269|PubMed:17609369,
CC ECO:0000269|PubMed:18400743, ECO:0000269|PubMed:18474359,
CC ECO:0000269|PubMed:8755875, ECO:0000269|PubMed:9864257}.
CC -!- PTM: Multiple forms of this protein exist in 2D-gels. The differences
CC between them has not been examined.
CC -!- MASS SPECTROMETRY: Mass=16100; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:1563797};
CC -!- DISRUPTION PHENOTYPE: Strains deleted for this gene show hypervirulence
CC upon intravenous inoculation in BALB/c mice.
CC {ECO:0000269|PubMed:16428728}.
CC -!- BIOTECHNOLOGY: In plasmid DNA-vaccinated mice, subsequent challenge
CC with this protein induces positive levels of antigen-specific IFN-gamma
CC and IL-2, indicating this might be a good vaccine candidate.
CC {ECO:0000269|PubMed:17145953}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S79751; AAB21317.1; -; Genomic_DNA.
DR EMBL; M76712; AAA25342.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44804.1; -; Genomic_DNA.
DR PIR; F70942; F70942.
DR RefSeq; NP_216547.1; NC_000962.3.
DR RefSeq; WP_003410189.1; NZ_NVQJ01000046.1.
DR AlphaFoldDB; P9WMK1; -.
DR SMR; P9WMK1; -.
DR IntAct; P9WMK1; 6.
DR STRING; 83332.Rv2031c; -.
DR MetOSite; P9WMK1; -.
DR PaxDb; P9WMK1; -.
DR DNASU; 887579; -.
DR GeneID; 887579; -.
DR KEGG; mtu:Rv2031c; -.
DR TubercuList; Rv2031c; -.
DR eggNOG; COG0071; Bacteria.
DR OMA; AGYDKGI; -.
DR PhylomeDB; P9WMK1; -.
DR PHI-base; PHI:4496; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0044183; F:protein folding chaperone; IDA:MTBBASE.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:MTBBASE.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MTBBASE.
DR GO; GO:0045926; P:negative regulation of growth; IMP:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0006457; P:protein folding; IDA:MTBBASE.
DR GO; GO:0009408; P:response to heat; IDA:MTBBASE.
DR GO; GO:0075136; P:response to host; IEP:MTBBASE.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
DR GO; GO:0010039; P:response to iron ion; IEP:MTBBASE.
DR GO; GO:0051409; P:response to nitrosative stress; IEP:MTBBASE.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Cell wall; Chaperone; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1563797,
FT ECO:0000269|PubMed:9864257"
FT CHAIN 2..144
FT /note="Alpha-crystallin"
FT /id="PRO_0000126011"
FT DOMAIN 33..143
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT CROSSLNK 64
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT CROSSLNK 85
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT CROSSLNK 114
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT CROSSLNK 132
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 144 AA; 16227 MW; A0C96872035CDDF8 CRC64;
MATTLPVQRH PRSLFPEFSE LFAAFPSFAG LRPTFDTRLM RLEDEMKEGR YEVRAELPGV
DPDKDVDIMV RDGQLTIKAE RTEQKDFDGR SEFAYGSFVR TVSLPVGADE DDIKATYDKG
ILTVSVAVSE GKPTEKHIQI RSTN
