ID   MEPA_HAEIN              Reviewed;         286 AA.
AC   P44566;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Penicillin-insensitive murein endopeptidase;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=mepA; OrderedLocusNames=HI_0197;
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: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-
CC       diamino-pimelyl amide bond that connects peptidoglycan strands. Likely
CC       plays a role in the removal of murein from the sacculus.
CC       {ECO:0000255|HAMAP-Rule:MF_01623}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M74 family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21866.1; -; Genomic_DNA.
DR   PIR; H64053; H64053.
DR   RefSeq; NP_438366.1; NC_000907.1.
DR   RefSeq; WP_005694094.1; NC_000907.1.
DR   AlphaFoldDB; P44566; -.
DR   SMR; P44566; -.
DR   STRING; 71421.HI_0197; -.
DR   MEROPS; M74.001; -.
DR   EnsemblBacteria; AAC21866; AAC21866; HI_0197.
DR   KEGG; hin:HI_0197; -.
DR   PATRIC; fig|71421.8.peg.202; -.
DR   eggNOG; COG3770; Bacteria.
DR   HOGENOM; CLU_052496_0_0_6; -.
DR   OMA; VRPWWGH; -.
DR   PhylomeDB; P44566; -.
DR   BioCyc; HINF71421:G1GJ1-208-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1380.10; -; 1.
DR   InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR   InterPro; IPR005073; Peptidase_M74.
DR   Pfam; PF03411; Peptidase_M74; 1.
DR   PIRSF; PIRSF018455; MepA; 1.
DR   SUPFAM; SSF55166; SSF55166; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Periplasm; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..286
FT                   /note="Penicillin-insensitive murein endopeptidase"
FT                   /id="PRO_0000028521"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31652 MW;  5D9EAF5FE0F86FD2 CRC64;
     MNKILLKTTI IFTALFSLNV VASPLDWQKV KRPIPSEDGK ASPIGSYTNG CIIGAQALPP
     KGEGYQVIRM NRNRYYGHPN MIQYLERLGQ RAKAAGLPTM LVGDIAMPGG GRFLTGHASH
     QMGLDADIWL RMGEMSDADA LNSDGKGLLV VDRKAQRVDE RVWNSNHATL IKLAAQDPNV
     TRIFVNPAIK VKLCQTAGND RGWLHKIRPW HGHNSHFHVR LTCPADASYC ENQAPVPAGD
     GCGDELYSWF EPPKPGTSVS KPKVTPPEPF LCQQILNSPN RREWLE