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Database: UniProt
Entry: A1THU2_MYCVP
LinkDB: A1THU2_MYCVP
Original site: A1THU2_MYCVP 
ID   A1THU2_MYCVP            Unreviewed;       292 AA.
AC   A1THU2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Peptidase M10 metallopeptidase domain-containing protein {ECO:0000259|Pfam:PF00413};
GN   OrderedLocusNames=Mvan_5986 {ECO:0000313|EMBL:ABM16742.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16742.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM16742.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000511; ABM16742.1; -; Genomic_DNA.
DR   RefSeq; WP_011783086.1; NZ_JACKSD010000159.1.
DR   AlphaFoldDB; A1THU2; -.
DR   STRING; 350058.Mvan_5986; -.
DR   MEROPS; M10.068; -.
DR   KEGG; mva:Mvan_5986; -.
DR   eggNOG; COG5549; Bacteria.
DR   HOGENOM; CLU_952554_0_0_11; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   Pfam; PF00413; Peptidase_M10; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..269
FT                   /note="Peptidase M10 metallopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00413"
FT   REGION          83..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  31066 MW;  968424FCFFC53BE1 CRC64;
     MTPLIRGRHG TATDLVAFRA RYSSPRPTGR HQPEPRSAGS LFAGFPALLI VVALLIGSAL
     LSHPEPAATT PYVAAGGAAP VADRPIQPSA APTPTPEQEP QQSVFSPIAR PAHPWLDEEP
     GGEPVAWACA PIGYRVVLEG APAGVEQLLA EATARISAVS GHQFRADRPL HWLEERSTPY
     VGITVAWVAR AEHPEASQDA IAIARTTTTP TPSGGSLYSA GKVHIFSDWP GAHRMNFTAN
     GVGPVMLHEL GHALGLGHSD DRDAMMHPTN LGVTTWSEPE RAALRYLRQS CR
//
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