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
//