MYCP1_MYCS2
ID MYCP1_MYCS2 Reviewed; 449 AA.
AC A0QNL1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Mycosin-1 {ECO:0000303|PubMed:23620593};
DE EC=3.4.21.- {ECO:0000269|PubMed:20227664};
DE AltName: Full=MycP1 protease {ECO:0000303|PubMed:20227664};
DE Flags: Precursor;
GN Name=mycP1 {ECO:0000303|PubMed:20227664};
GN OrderedLocusNames=MSMEG_0083 {ECO:0000312|EMBL:ABK70081.1},
GN MSMEI_0081 {ECO:0000312|EMBL:AFP36563.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-334.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=20227664; DOI=10.1016/j.chom.2010.02.006;
RA Ohol Y.M., Goetz D.H., Chan K., Shiloh M.U., Craik C.S., Cox J.S.;
RT "Mycobacterium tuberculosis MycP1 protease plays a dual role in regulation
RT of ESX-1 secretion and virulence.";
RL Cell Host Microbe 7:210-220(2010).
RN [5] {ECO:0007744|PDB:4J94, ECO:0007744|PDB:4KPG}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 24-407, FUNCTION AS A PROTEASE,
RP DOMAIN, MUTAGENESIS OF SER-334, ACTIVE SITES, AND DISULFIDE BONDS.
RX PubMed=23620593; DOI=10.1074/jbc.m113.462036;
RA Solomonson M., Huesgen P.F., Wasney G.A., Watanabe N., Gruninger R.J.,
RA Prehna G., Overall C.M., Strynadka N.C.;
RT "Structure of the mycosin-1 protease from the mycobacterial ESX-1 protein
RT type VII secretion system.";
RL J. Biol. Chem. 288:17782-17790(2013).
RN [6] {ECO:0007744|PDB:4KB5, ECO:0007744|PDB:4M1Z}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 24-422, DISULFIDE BONDS, ACTIVE
RP SITES, AND DOMAIN.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=24248472; DOI=10.1007/s13238-013-3089-7;
RA Sun D., Liu Q., He Y., Wang C., Wu F., Tian C., Zang J.;
RT "The putative propeptide of MycP1 in mycobacterial type VII secretion
RT system does not inhibit protease activity but improves protein stability.";
RL Protein Cell 4:921-931(2013).
CC -!- FUNCTION: May play a dual role in regulation of ESX-1 secretion and
CC virulence. Acts as a protease that cleaves EspB.
CC {ECO:0000269|PubMed:20227664, ECO:0000269|PubMed:23620593}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O05461};
CC Single-pass membrane protein {ECO:0000255}. Note=Cell wall-associated.
CC {ECO:0000250|UniProtKB:O05461}.
CC -!- DOMAIN: The N-terminal extension wraps intimately around the catalytic
CC domain where, tethered by a disulfide bond, it forms additional
CC interactions with a unique extended loop that protrudes from the
CC catalytic core. It might contribute to the conformational stability of
CC the active site cleft and surrounding regions.
CC {ECO:0000269|PubMed:23620593, ECO:0000269|PubMed:24248472}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant fails to secrete EsxA.
CC {ECO:0000269|PubMed:20227664}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70081.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP36563.1; -; Genomic_DNA.
DR RefSeq; WP_011726654.1; NZ_SIJM01000048.1.
DR RefSeq; YP_884499.1; NC_008596.1.
DR PDB; 4J94; X-ray; 1.86 A; A=24-407.
DR PDB; 4KB5; X-ray; 2.15 A; A=24-422.
DR PDB; 4KPG; X-ray; 2.15 A; A=24-407.
DR PDB; 4M1Z; X-ray; 2.25 A; A/B=63-422, C/D=403-422.
DR PDBsum; 4J94; -.
DR PDBsum; 4KB5; -.
DR PDBsum; 4KPG; -.
DR PDBsum; 4M1Z; -.
DR AlphaFoldDB; A0QNL1; -.
DR SMR; A0QNL1; -.
DR STRING; 246196.MSMEI_0081; -.
DR MEROPS; S08.131; -.
DR PRIDE; A0QNL1; -.
DR EnsemblBacteria; ABK70081; ABK70081; MSMEG_0083.
DR EnsemblBacteria; AFP36563; AFP36563; MSMEI_0081.
DR GeneID; 66738274; -.
DR KEGG; msg:MSMEI_0081; -.
DR KEGG; msm:MSMEG_0083; -.
DR PATRIC; fig|246196.19.peg.81; -.
DR eggNOG; COG1404; Bacteria.
DR OMA; WANDYLR; -.
DR OrthoDB; 923655at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR023834; T7SS_pept_S8A_mycosin.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR TIGRFAMs; TIGR03921; T7SS_mycosin; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..449
FT /note="Mycosin-1"
FT /id="PRO_5007633026"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 66..389
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:23620593, ECO:0000305|PubMed:24248472"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:23620593, ECO:0000305|PubMed:24248472"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000305|PubMed:23620593, ECO:0000305|PubMed:24248472"
FT DISULFID 51..120
FT /evidence="ECO:0000269|PubMed:23620593,
FT ECO:0000269|PubMed:24248472, ECO:0007744|PDB:4J94,
FT ECO:0007744|PDB:4KB5, ECO:0007744|PDB:4KPG"
FT DISULFID 206..244
FT /evidence="ECO:0000269|PubMed:23620593,
FT ECO:0000269|PubMed:24248472, ECO:0007744|PDB:4J94,
FT ECO:0007744|PDB:4KB5, ECO:0007744|PDB:4KPG"
FT MUTAGEN 334
FT /note="S->A: Lack of protease activity. Increases EsxA
FT secretion."
FT /evidence="ECO:0000269|PubMed:20227664,
FT ECO:0000269|PubMed:23620593"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:4J94"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4KB5"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4KPG"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4KB5"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4J94"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4J94"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4KPG"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:4J94"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:4J94"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:4J94"
SQ SEQUENCE 449 AA; 46454 MW; 9E152A7C54499766 CRC64;
MQRVAVMVLA VLLALFSAPP AWAIDPPVID AGAVPPDETG PDQPTEQRKI CATPTVMPNS
NFADRPWAND YLRIQEAQKF ATGAGVTVAV IDTGVNGSPR VPAEPGGDFV DAAGNGMSDC
DAHGTMTAAI IGGRPSPTDG FVGMAPDVRL LSLRQTSVAF QPKGARQDPN DPNTTQTAGS
IRSLARSVVH AANLGAQVIN ISEAACYKVT RRIDETSLGA AINYAVNVKG AVIVVAAGNT
GQDCSQNPPP DPSVPSDPRG WREVQTIVSP AWYDPLVLTV GSIGQNGQPS NFSMSGPWVG
AAAPGENLTS LGYDGQPVNA TPGEDGPVPL NGTSFSAAYV SGLAALVKQR FPDLTPAQII
NRITATARHP GGGVDNYVGA GVIDPVAALT WEIPDGPEKA PFRVKEVPPP VYIPPPDRGP
ITAVVIAGAT LAFALGIGAL ARRALRRKQ
