ID   Y3671_MYCTO             Reviewed;         397 AA.
AC   P9WHR8; L0TDG7; O69639; Q7D538;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Serine protease MT3772;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=MT3772;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Required for M.tuberculosis resistance to oxidative stress in
CC       addition to its role in resistance to acid, which is essential for
CC       virulence. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Disulfide bond increases the proteolytic activity by
CC       stabilizing the protease in the conformation in which the active site
CC       residues are properly positioned for substrate binding and catalysis.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48139.1; -; Genomic_DNA.
DR   PIR; H70789; H70789.
DR   RefSeq; WP_003900734.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHR8; -.
DR   SMR; P9WHR8; -.
DR   MEROPS; S01.513; -.
DR   EnsemblBacteria; AAK48139; AAK48139; MT3772.
DR   KEGG; mtc:MT3772; -.
DR   PATRIC; fig|83331.31.peg.4062; -.
DR   HOGENOM; CLU_043139_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR003825; Colicin-V_CvpA.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF02674; Colicin_V; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Disulfide bond; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..397
FT                   /note="Serine protease MT3772"
FT                   /id="PRO_0000428135"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10079"
FT   SITE            160..161
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..395
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  40721 MW;  2759E1941B9C7F1C CRC64;
     MTPSQWLDIA VLAVAFIAAI SGWRAGALGS MLSFGGVLLG ATAGVLLAPH IVSQISAPRA
     KLFAALFLIL ALVVVGEVAG VVLGRAVRGA IRNRPIRLID SVIGVGVQLV VVLTAAWLLA
     MPLTQSKEQP ELAAAVKGSR VLARVNEAAP TWLKTVPKRL SALLNTSGLP AVLEPFSRTP
     VIPVASPDPA LVNNPVVAAT EPSVVKIRSL APRCQKVLEG TGFVISPDRV MTNAHVVAGS
     NNVTVYAGDK PFEATVVSYD PSVDVAILAV PHLPPPPLVF AAEPAKTGAD VVVLGYPGGG
     NFTATPARIR EAIRLSGPDI YGDPEPVTRD VYTIRADVEQ GDSGGPLIDL NGQVLGVVFG
     AAIDDAETGF VLTAGEVAGQ LAKIGATQPV GTGACVS