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Database: UniProt
Entry: A0QSV6_MYCS2
LinkDB: A0QSV6_MYCS2
Original site: A0QSV6_MYCS2 
ID   A0QSV6_MYCS2            Unreviewed;       550 AA.
AC   A0QSV6;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Kumamolisin {ECO:0000313|EMBL:ABK75602.1};
GN   OrderedLocusNames=MSMEG_1617 {ECO:0000313|EMBL:ABK75602.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK75602.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK75602.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
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.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP000480; ABK75602.1; -; Genomic_DNA.
DR   RefSeq; WP_011727775.1; NZ_SIJM01000023.1.
DR   RefSeq; YP_885994.1; NC_008596.1.
DR   AlphaFoldDB; A0QSV6; -.
DR   STRING; 246196.MSMEG_1617; -.
DR   MEROPS; S53.004; -.
DR   PaxDb; 246196-MSMEI_1579; -.
DR   GeneID; 66733070; -.
DR   KEGG; msm:MSMEG_1617; -.
DR   PATRIC; fig|246196.19.peg.1604; -.
DR   eggNOG; COG4934; Bacteria.
DR   OrthoDB; 3480681at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          184..545
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   550 AA;  57980 MW;  23D3B8A32D2C617A CRC64;
     MAGTTRHVGV SIRNPGGFRH WHTHWSLALI MIGALLISVF RITSGPDGHG PAEIAGPYAH
     LLAASTDLGP ADGGPVQLTV TLDGSPEALT SWARERGLSV RWRHGDTWAI VEGPPADMAA
     AFEVDIHDYR GRRGQEFYAS PQQPSIPEPV RSEVTEVGRI LGYTPYRMNT PDLQHLPAEV
     PDRGLTPQLL LNTYNLRGLA EQGYTGKGQT IVIFAFDGFD QADLDTYADT FDLPRFTPIL
     VGGQPSTPRG ETTMDLQVAH AIAPDARKVV VNARPTVQGD GAYEKIGQML EDADRQFPGA
     VWSFSIGWGC DKLITAADLA PVRSALAAAH TRGTTAFNAS GDLAGLECKG GQDWSSAPGD
     DDIGLDSVAS LPEITDVGGT TLSTTADGAW LAEQAWFDVP LSQGTGGGVS ALFDRPDWQQ
     GFSAPDDGGA QRRLTPDIAA VADPFTGVKI VLNNQVLVGG GTSQAAPLWA GIAAVMNQYL
     VANGGRAIGD LNPMLYQIAR GAPLPAFRDV TLGGNAVATA GPGYDLVTGL GTPDTENLVK
     NLLVLQKANP
//
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