ID   SPI_MYCTU               Reviewed;         130 AA.
AC   O50393; F2GEB0; I6YFX5; Q7D5M4;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Serine protease inhibitor Rv3364c {ECO:0000305|PubMed:22275911};
GN   OrderedLocusNames=Rv3364c {ECO:0000312|EMBL:CCP46185.1},
GN   LH57_18375 {ECO:0000312|EMBL:AIR16157.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH HUMAN
RP   CATHEPSIN G.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=22275911; DOI=10.3389/fmicb.2011.00281;
RA   Danelishvili L., Everman J.L., McNamara M.J., Bermudez L.E.;
RT   "Inhibition of the plasma-membrane-associated serine protease cathepsin G
RT   by Mycobacterium tuberculosis Rv3364c suppresses caspase-1 and pyroptosis
RT   in macrophages.";
RL   Front. Microbiol. 2:281-281(2011).
RN   [4]
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: Effector protein that binds to the host serine protease
CC       cathepsin G on the macrophage cell membrane, inhibiting its enzymatic
CC       activity and the downstream activation of caspase-1-dependent
CC       apoptosis. Thus prevents macrophage pyroptosis and helps M.tuberculosis
CC       survival within host cells. {ECO:0000269|PubMed:22275911}.
CC   -!- SUBUNIT: Interacts with human cathepsin G protein.
CC       {ECO:0000269|PubMed:22275911}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22275911}. Host
CC       cytoplasm {ECO:0000269|PubMed:22275911}. Note=Is translocated into the
CC       cytoplasm of macrophages. {ECO:0000269|PubMed:22275911}.
CC   -!- INDUCTION: Component of the signal transduction operon Rv3361c-Rv3365c
CC       that is highly up-regulated during M.tuberculosis infection of
CC       macrophages. {ECO:0000269|PubMed:22275911}.
CC   -!- SIMILARITY: Belongs to the mycobacterial serine protease inhibitor
CC       Rv3364c family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46185.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR16157.1; -; Genomic_DNA.
DR   RefSeq; NP_217881.1; NC_000962.3.
DR   RefSeq; WP_003417776.1; NZ_NVQJ01000052.1.
DR   AlphaFoldDB; O50393; -.
DR   SMR; O50393; -.
DR   STRING; 83332.Rv3364c; -.
DR   PaxDb; O50393; -.
DR   PRIDE; O50393; -.
DR   GeneID; 45427363; -.
DR   GeneID; 888085; -.
DR   KEGG; mtu:Rv3364c; -.
DR   PATRIC; fig|83332.111.peg.3753; -.
DR   TubercuList; Rv3364c; -.
DR   eggNOG; COG2018; Bacteria.
DR   HOGENOM; CLU_094585_0_1_11; -.
DR   OMA; SDGFPRD; -.
DR   PhylomeDB; O50393; -.
DR   Reactome; R-HSA-9635465; Suppression of apoptosis.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004942; Roadblock/LAMTOR2_dom.
DR   Pfam; PF03259; Robl_LC7; 1.
DR   SMART; SM00960; Robl_LC7; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Virulence.
FT   CHAIN           1..130
FT                   /note="Serine protease inhibitor Rv3364c"
FT                   /id="PRO_0000438185"
SQ   SEQUENCE   130 AA;  13440 MW;  7BE358D961B3AAC1 CRC64;
     MKARLPDSPL DWLVSKFARE VPGVAHALLV SVDGLPVAAS EHLPRERADQ LAAVTSGLAS
     LAGGAAQLFD GGQVLQSVVE MQNGYLLLMQ VGDGSALAAL AATGCDIGQI GYEMAILVER
     VGGVVQSCRR