ID   Y409_HAEIN              Reviewed;         475 AA.
AC   P44693;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Uncharacterized metalloprotease HI_0409;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=HI_0409;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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: In the central section; belongs to the OapA family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M23B
CC       family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22068.1; -; Genomic_DNA.
DR   PIR; F64151; F64151.
DR   RefSeq; NP_438571.1; NC_000907.1.
DR   AlphaFoldDB; P44693; -.
DR   SMR; P44693; -.
DR   STRING; 71421.HI_0409; -.
DR   MEROPS; M23.011; -.
DR   EnsemblBacteria; AAC22068; AAC22068; HI_0409.
DR   KEGG; hin:HI_0409; -.
DR   PATRIC; fig|71421.8.peg.428; -.
DR   eggNOG; COG0739; Bacteria.
DR   HOGENOM; CLU_026846_3_2_6; -.
DR   OMA; GPHVCYR; -.
DR   PhylomeDB; P44693; -.
DR   BioCyc; HINF71421:G1GJ1-424-MON; -.
DR   Proteomes; UP000000579; 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:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IBA:GO_Central.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR045834; Csd3_N2.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR007340; Opacity-associatedA.
DR   InterPro; IPR016047; Peptidase_M23.
DR   Pfam; PF19425; Csd3_N2; 1.
DR   Pfam; PF04225; OapA; 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..475
FT                   /note="Uncharacterized metalloprotease HI_0409"
FT                   /id="PRO_0000165905"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          55..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  53255 MW;  143C10F92233939D CRC64;
     MPVQHVKLAR DRRKKRAYIK VGVFFVAILL ILTGILLTIK SKPEENSIFS TFDSGEYHEL
     NTSPNENSTA LQPDENATSY DDELQAKDDE VDEVKLSSDD LDTLPQHAQD ALNGLLDAAD
     QAIRITDQFS YTVTEGDTLK DVLVLSGLDD SSVQPLIALD PELAHLKAGQ QFYWILDKND
     NLEYLNWLVS EKEERIYERL EDGKFKRQVI EKKSIWRKEV LKGEIQNSLN SSLREKGLDT
     RQISQLSNAL QWQVSLRKLK KGTQFAILVS REYLGDKLTG QGNVEALRIS SGGKNYYAVQ
     AANGRYYNQQ GETLGKGFAR YPLQRQARVS SPFNPNRRHP VTGRIRPHKG VDFSVSQGTP
     VIAPADGTVE KVAYQAGGAG RYVMLRHGRE YQTVYMHLSK SLVKAGQTVK KGERIALSGN
     TGISTGPHLH YEFHINGRAV NPLTVKLPGT SSGMTSAERK QFLVRVREAE RMLKP