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HTPX_MYCTU
ID   HTPX_MYCTU              Reviewed;         286 AA.
AC   P9WHS5; L0T459; O06429; P65815;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Protease HtpX homolog;
DE            EC=3.4.24.-;
GN   Name=htpX; OrderedLocusNames=Rv0563; ORFNames=MTCY25D10.42, MTV039.01;
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 [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   [2]
RP   BIOTECHNOLOGY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=18342411; DOI=10.1016/j.vaccine.2008.02.023;
RA   Brun P., Zumbo A., Castagliuolo I., Delogu G., Manfrin F., Sali M.,
RA   Fadda G., Grillot-Courvalin C., Palu G., Manganelli R.;
RT   "Intranasal delivery of DNA encoding antigens of Mycobacterium tuberculosis
RT   by non-pathogenic invasive Escherichia coli.";
RL   Vaccine 26:1934-1941(2008).
RN   [3]
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Mice immunized with recombinant bacteria carrying a DNA
CC       vaccine encoding HtpX were significantly protected from challenge with
CC       M.tuberculosis, indicating this might be a good vaccine candidate.
CC       {ECO:0000269|PubMed:18342411}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43301.1; -; Genomic_DNA.
DR   PIR; F70549; F70549.
DR   RefSeq; NP_215077.1; NC_000962.3.
DR   RefSeq; WP_003402959.1; NZ_NVQJ01000036.1.
DR   AlphaFoldDB; P9WHS5; -.
DR   STRING; 83332.Rv0563; -.
DR   PaxDb; P9WHS5; -.
DR   DNASU; 887649; -.
DR   GeneID; 887649; -.
DR   KEGG; mtu:Rv0563; -.
DR   TubercuList; Rv0563; -.
DR   eggNOG; COG0501; Bacteria.
DR   OMA; AVCCTEG; -.
DR   PhylomeDB; P9WHS5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..286
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138875"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  30682 MW;  9D1ED210A449465D CRC64;
     MTWHPHANRL KTFLLLVGMS ALIVAVGALF GRTALMLAAL FAVGMNVYVY FNSDKLALRA
     MHAQPVSELQ APAMYRIVRE LATSAHQPMP RLYISDTAAP NAFATGRNPR NAAVCCTTGI
     LRILNERELR AVLGHELSHV YNRDILISCV AGALAAVITA LANMAMWAGM FGGNRDNANP
     FALLLVALLG PIAATVIRMA VSRSREYQAD ESGAVLTGDP LALASALRKI SGGVQAAPLP
     PEPQLASQAH LMIANPFRAG ERIGSLFSTH PPIEDRIRRL EAMARG
 
 
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