ID   Y296_BUCBP              Reviewed;         376 AA.
AC   Q89AI9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Uncharacterized metalloprotease bbp_296;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=bbp_296;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27021.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q89AI9; -.
DR   SMR; Q89AI9; -.
DR   STRING; 224915.bbp_296; -.
DR   MEROPS; M23.011; -.
DR   EnsemblBacteria; AAO27021; AAO27021; bbp_296.
DR   KEGG; bab:bbp_296; -.
DR   eggNOG; COG0739; Bacteria.
DR   HOGENOM; CLU_735034_0_0_6; -.
DR   OMA; NNECMEV; -.
DR   Proteomes; UP000000601; 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; IPR016047; Peptidase_M23.
DR   Pfam; PF19425; Csd3_N2; 1.
DR   Pfam; PF01551; Peptidase_M23; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..376
FT                   /note="Uncharacterized metalloprotease bbp_296"
FT                   /id="PRO_0000026828"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   376 AA;  43833 MW;  1DB8AD65D9B5A2BB CRC64;
     MTKCNIFNMI FLKFSNAFIK KIKYLSIISI ISVFLLNSSI VYSCSKIILI FDNNFKENNK
     NILNKLVLPI KNIILKGTSN LEFNDYLLKL SNFYGSPIHK CIYNFPYKKL QNNNLNNLKY
     IIFKSKIDNN FIKNMQYLNV SNDNIDNVVR CIKLELKIHQ LKQDHKCNIL IQNNSFLKHN
     IVQKNIILSF EIPYNTKNIY GFFTKKNKFF DVHGISSAPI FLKFPFLKKY RISSKFNPNR
     FNPITKKNSP HQGIDFAMPI GTPILSIGDG VILNAKFSIQ AGNYITIQHN CSYITKYMHL
     KKILVKIGDK VKMRDKIGLS GNTGYSTGPH LHYEVWLHKK VINPKNLKTR ECLIKKNLKE
     HINFSNIIIT QFEIFK