MYCP4_MYCTU
ID MYCP4_MYCTU Reviewed; 455 AA.
AC I6YC58;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mycosin-4 {ECO:0000303|PubMed:10974545};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:O05461};
DE AltName: Full=MycP4 protease {ECO:0000305};
DE Flags: Precursor;
GN Name=mycP4 {ECO:0000303|PubMed:10974545};
GN OrderedLocusNames=Rv3449 {ECO:0000312|EMBL:CCP46271.1};
GN ORFNames=LH57_18835 {ECO:0000312|EMBL:AIR16244.1};
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 INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=10974545; DOI=10.1016/s0378-1119(00)00277-8;
RA Brown G.D., Dave J.A., Gey van Pittius N.C., Stevens L., Ehlers M.R.,
RA Beyers A.D.;
RT "The mycosins of Mycobacterium tuberculosis H37Rv: a family of subtilisin-
RT like serine proteases.";
RL Gene 254:147-155(2000).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed during growth in culture.
CC {ECO:0000269|PubMed:10974545}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; CP009480; AIR16244.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46271.1; -; Genomic_DNA.
DR RefSeq; NP_217966.1; NC_000962.3.
DR RefSeq; WP_003418331.1; NZ_NVQJ01000065.1.
DR AlphaFoldDB; I6YC58; -.
DR SMR; I6YC58; -.
DR STRING; 83332.Rv3449; -.
DR MEROPS; S08.131; -.
DR PaxDb; I6YC58; -.
DR PRIDE; I6YC58; -.
DR DNASU; 887602; -.
DR GeneID; 887602; -.
DR KEGG; mtu:Rv3449; -.
DR PATRIC; fig|83332.111.peg.3844; -.
DR TubercuList; Rv3449; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_13_1_11; -.
DR OMA; TQDCDAH; -.
DR PhylomeDB; I6YC58; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
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.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..455
FT /note="Mycosin-4"
FT /id="PRO_5007674266"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 74..384
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 389..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 329
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 455 AA; 46016 MW; 7DC901D25C07C8A8 CRC64;
MTTSRTLRLL VVSALATLSG LGTPVAHAVS PPPIDERWLP ESALPAPPRP TVQREVCTEV
TAESGRAFGR AERSAQLADL DQVWRLTRGA GQRVAVIDTG VARHRRLPKV VAGGDYVFTG
DGTADCDAHG TLVAGIIAAA PDAQSDNFSG VAPDVTLISI RQSSSKFAPV GDPSSTGVGD
VDTMAKAVRT AADLGASVIN ISSIACVPAA AAPDDRALGA ALAYAVDVKN AVIVAAAGNT
GGAAQCPPQA PGVTRDSVTV AVSPAWYDDY VLTVGSVNAQ GEPSAFTLAG PWVDVAATGE
AVTSLSPFGD GTVNRLGGQH GSIPISGTSY AAPVVSGLAA LIRARFPTLT ARQVMQRIES
TAHHPPAGWD PLVGNGTVDA LAAVSSDSIP QAGTATSDPA PVAVPVPRRS TPGPSDRRAL
HTAFAGAAIC LLALMATLAT ASRRLRPGRN GIAGD
