HTRA1_MYCTU
ID HTRA1_MYCTU Reviewed; 528 AA.
AC O06291; F2GFU0; I6Y608; Q8VK49;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable serine protease HtrA1 {ECO:0000305};
DE EC=3.4.21.107 {ECO:0000250|UniProtKB:P0C0V0};
DE AltName: Full=High-temperature requirement A protease {ECO:0000303|PubMed:30198900};
GN Name=htrA1 {ECO:0000303|PubMed:30198900};
GN Synonyms=degP {ECO:0000303|PubMed:30198900},
GN htrA {ECO:0000303|PubMed:15952732};
GN OrderedLocusNames=Rv1223 {ECO:0000312|EMBL:CCP43979.1};
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 SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15952732; DOI=10.1021/pr0500049;
RA Xiong Y., Chalmers M.J., Gao F.P., Cross T.A., Marshall A.G.;
RT "Identification of Mycobacterium tuberculosis H37Rv integral membrane
RT proteins by one-dimensional gel electrophoresis and liquid chromatography
RT electrospray ionization tandem mass spectrometry.";
RL J. Proteome Res. 4:855-861(2005).
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).
RN [4] {ECO:0007744|PDB:5ZVJ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 206-528 OF MUTANT ALA-387,
RP SUBUNIT, AND DOMAIN.
RX PubMed=30198900; DOI=10.1107/s205979831800952x;
RA Singh K.H., Yadav S., Kumar D., Biswal B.K.;
RT "The crystal structure of an essential high-temperature requirement protein
RT HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique
RT features.";
RL Acta Crystallogr. D 74:906-921(2018).
RN [5] {ECO:0007744|PDB:6IEO}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 223-528, FUNCTION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=30511675; DOI=10.1107/s2053230x18016217;
RA Gupta A.K., Behera D., Gopal B.;
RT "The crystal structure of Mycobacterium tuberculosis high-temperature
RT requirement A protein reveals an autoregulatory mechanism.";
RL Acta Crystallogr. F Struct. Biol. Commun. 74:803-809(2018).
CC -!- FUNCTION: Essential protein that may act as a regulatory protease that
CC is conditionally activated upon appropriate environmental triggers.
CC {ECO:0000269|PubMed:30511675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC Evidence={ECO:0000250|UniProtKB:P0C0V0};
CC -!- SUBUNIT: The C-terminal region exhibits both monomeric and trimeric
CC forms in solution. {ECO:0000269|PubMed:30198900,
CC ECO:0000269|PubMed:30511675}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15952732}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The periplasmic region consists of a protease domain (PD) and a
CC PDZ domain, connected by a ten-residue linker (PubMed:30198900).
CC Interactions between the PDZ domain and the catalytic domain lead to an
CC inactive conformation (PubMed:30511675). {ECO:0000269|PubMed:30198900,
CC ECO:0000269|PubMed:30511675}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43979.1; -; Genomic_DNA.
DR RefSeq; NP_215739.2; NC_000962.3.
DR RefSeq; WP_003898779.1; NC_000962.3.
DR PDB; 5ZVJ; X-ray; 2.70 A; A=206-528.
DR PDB; 6IEO; X-ray; 1.83 A; A=223-528.
DR PDBsum; 5ZVJ; -.
DR PDBsum; 6IEO; -.
DR AlphaFoldDB; O06291; -.
DR SMR; O06291; -.
DR STRING; 83332.Rv1223; -.
DR PaxDb; O06291; -.
DR PRIDE; O06291; -.
DR DNASU; 888912; -.
DR GeneID; 45425193; -.
DR GeneID; 888912; -.
DR KEGG; mtu:Rv1223; -.
DR PATRIC; fig|83332.111.peg.1367; -.
DR TubercuList; Rv1223; -.
DR eggNOG; COG0265; Bacteria.
DR OMA; DDPWRNP; -.
DR PhylomeDB; O06291; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF13180; PDZ_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Protease; Reference proteome; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..528
FT /note="Probable serine protease HtrA1"
FT /id="PRO_0000450814"
FT TOPO_DOM 1..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30198900"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..528
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:30198900"
FT DOMAIN 426..487
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P0C0V0"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:6IEO"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:6IEO"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:6IEO"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 348..362
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 371..380
FT /evidence="ECO:0007829|PDB:6IEO"
FT TURN 384..388
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 421..434
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 467..471
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:6IEO"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5ZVJ"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:6IEO"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:6IEO"
SQ SEQUENCE 528 AA; 54190 MW; F9C4C6FD6C87BCB3 CRC64;
MDTRVDTDNA MPARFSAQIQ NEDEVTSDQG NNGGPNGGGR LAPRPVFRPP VDPASRQAFG
RPSGVQGSFV AERVRPQKYQ DQSDFTPNDQ LADPVLQEAF GRPFAGAESL QRHPIDAGAL
AAEKDGAGPD EPDDPWRDPA AAAALGTPAL AAPAPHGALA GSGKLGVRDV LFGGKVSYLA
LGILVAIALV IGGIGGVIGR KTAEVVDAFT TSKVTLSTTG NAQEPAGRFT KVAAAVADSV
VTIESVSDQE GMQGSGVIVD GRGYIVTNNH VISEAANNPS QFKTTVVFND GKEVPANLVG
RDPKTDLAVL KVDNVDNLTV ARLGDSSKVR VGDEVLAVGA PLGLRSTVTQ GIVSALHRPV
PLSGEGSDTD TVIDAIQTDA SINHGNSGGP LIDMDAQVIG INTAGKSLSD SASGLGFAIP
VNEMKLVANS LIKDGKIVHP TLGISTRSVS NAIASGAQVA NVKAGSPAQK GGILENDVIV
KVGNRAVADS DEFVVAVRQL AIGQDAPIEV VREGRHVTLT VKPDPDST
