ID   PMBA_HAEIN              Reviewed;         451 AA.
AC   P45077;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Metalloprotease PmbA homolog;
DE            EC=3.4.-.-;
GN   Name=pmbA; OrderedLocusNames=HI_1152;
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   -!- FUNCTION: Probable metalloprotease. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22807.1; -; Genomic_DNA.
DR   PIR; C64186; C64186.
DR   RefSeq; NP_439310.1; NC_000907.1.
DR   RefSeq; WP_005693467.1; NC_000907.1.
DR   AlphaFoldDB; P45077; -.
DR   SMR; P45077; -.
DR   STRING; 71421.HI_1152; -.
DR   EnsemblBacteria; AAC22807; AAC22807; HI_1152.
DR   KEGG; hin:HI_1152; -.
DR   PATRIC; fig|71421.8.peg.1202; -.
DR   eggNOG; COG0312; Bacteria.
DR   HOGENOM; CLU_026425_0_0_6; -.
DR   OMA; LYRKSTF; -.
DR   PhylomeDB; P45077; -.
DR   BioCyc; HINF71421:G1GJ1-1185-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2290.10; -; 1.
DR   InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR   InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR   InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR   InterPro; IPR035068; TldD/PmbA_N.
DR   InterPro; IPR036059; TldD/PmbA_sf.
DR   Pfam; PF01523; PmbA_TldD; 1.
DR   Pfam; PF19289; PmbA_TldD_C; 1.
DR   Pfam; PF19290; PmbA_TldD_M; 1.
DR   SUPFAM; SSF111283; SSF111283; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metalloprotease; Protease; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Metalloprotease PmbA homolog"
FT                   /id="PRO_0000142353"
SQ   SEQUENCE   451 AA;  48498 MW;  8C8E080C0A297700 CRC64;
     MKPAENSTAL LKAQEQELRQ AVSFAVELAT KAGASAEVAV TKVSGLSVSA RLQEIENVEF
     TNDGALGISV YMGQQKGNAS TSDLSESAIK NAVEAALAIA KYTSPDDCTG LADKDLMAFD
     APDLELYHAA DIDVDKATEL ALQAEQAALQ ADERIINSNG ASFNSHTGVK VYGNSHGMLQ
     SYLSSRYSLS CSVIGGVEDA LENDYEYTIS REFDKLQSPI WVGENCAKKV VSRLNPQKLS
     TREVPVIFLN DVATGIISHF AAAISGGSLY RKSSFLLDHL GKQVLPDWFS ISERPHLLRR
     LASTPFDSEG VRTQDREIVE NGILQTYLVT SYSGKKLGMS STGHAGGIHN WLVKPNLTGG
     LTALLRQMGT GLLVTDVMGQ GVNIVTGDYS RGASGFWVEN GEIQYPVAEI TIAGQLQDML
     KNMLAVADDI EHRSNIQTGS ILLDKMKISG N