ID   B8L9H7_9GAMM            Unreviewed;       712 AA.
AC   B8L9H7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   SubName: Full=Peptidase family M3 {ECO:0000313|EMBL:EED40665.1};
GN   ORFNames=SSKA14_3688 {ECO:0000313|EMBL:EED40665.1};
OS   Stenotrophomonas sp. SKA14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=391601 {ECO:0000313|EMBL:EED40665.1};
RN   [1] {ECO:0000313|EMBL:EED40665.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA14 {ECO:0000313|EMBL:EED40665.1};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; DS999412; EED40665.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8L9H7; -.
DR   HOGENOM; CLU_001805_4_0_6; -.
DR   Proteomes; UP000003991; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          254..706
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   712 AA;  78250 MW;  623EB740E8E825DF CRC64;
     MTLGLALPAY SAGAATPAAS TIAQQANPFF ADSPLPLHFP QFDRIKDSDF APAFDAGMAQ
     QLKEVEAIAN NKAKPTFDNT IIALEKSGDI LDRATTVFFS LVGADTNDTR KKLQADYSAK
     FAAHSDAIAL NGKLFARIQA LYDTRSQLGL DAEGVRLVEK YYDNYVRAGA KLSEADKATL
     KEMNAELANL GTKFSQNVQS EVNASAITVD DVKELAGLSK EQIAAAAEAA KARGLEGKYV
     ITLLNTTGQP PLTNLANRAL RQKIYQASVS RGSRGGEFDN TALVSRIMQL RADKAKLMGF
     ANFAAYNLTN QTAKTPEAVN AMLGKLAPAA VANAKREAAD LQAMIDQEQK AAGKKTFQLE
     PWDWAFYSEK VRQAKYNFDE SQLKPYFEMK NVLENGVFYA AGQEFGLTFK QRTDLPVYHD
     DVTVYDVFDA DGSQLAIFIF DPYARASKRG GAWMNSYVSQ SKLTGFKPVV ANHLNIPKPP
     AGQPTLLTWD EVNTTFHEFG HALHGMFSNV KYPYFSGTSV PRDFVEFPSQ VNEMWSDNPA
     ILKNYAKHYQ NGSAMPQALL DKVLAAAKFN QGFATTEYLG AAMLDQRWHQ IGADQVPAAK
     DVMAFERAAL EKDGIYYAPV PPRYKTPYFS HIMGGYSAGY YAYIWSEVLD ANTQKWFKDN
     GGLSRKNGDH FRATLLSKGG SVDAMQLFRD FAGHEPQIEP LLEKRGLTGA GN
//