ID   Y310_BUCAP              Reviewed;         415 AA.
AC   Q8K9M4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Uncharacterized metalloprotease BUsg_310;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=BUsg_310;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67864.1; -; Genomic_DNA.
DR   RefSeq; WP_011053831.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9M4; -.
DR   SMR; Q8K9M4; -.
DR   STRING; 198804.BUsg_310; -.
DR   MEROPS; M23.011; -.
DR   EnsemblBacteria; AAM67864; AAM67864; BUsg_310.
DR   KEGG; bas:BUsg_310; -.
DR   eggNOG; COG0739; Bacteria.
DR   HOGENOM; CLU_026846_0_2_6; -.
DR   OMA; EIWINHR; -.
DR   OrthoDB; 1891666at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR045834; Csd3_N2.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF19425; Csd3_N2; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..415
FT                   /note="Uncharacterized metalloprotease BUsg_310"
FT                   /id="PRO_0000026827"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          77..122
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  48878 MW;  53C92D536FF4479D CRC64;
     MQQIYKIIFL SFNQDFFYKT IKILINIILI VIFILLSSCN FLTDKKAFFL NKEFSQKEKE
     FKRLKEKKEY LKKHTIHKHI FSYGNTISIF LKKSGVKIND ILKLIKIDKN LNNITIGQKI
     VCKVDNLGNL IKLKWYISKF QKKIYKRYKN TFKFIKYTYD SFLEKKSIYI KKNSNFFKSA
     YQSGLNKSEI NSVIKAIEWQ INFNKLHIGS KFNVIFLNQK TKNKKILLGV KLDNLDRKYF
     SIRAFNGKFY DSDGFNKSEE LINFSFLKKY RISSPFNLRR VNPVTHRISR HLGIDLAMPQ
     GTPVIATSSG KIIKAQFNKI AGFYISLKNK NYYTTRYMHL KKILVKVGQK IKKGEKIALS
     GNTGRTTGPH LHYEIWINHR AINPIKAEYI LSTQLTKSER IKYLKESKNI LSKLK