ID   Y084_NEIMA              Reviewed;         446 AA.
AC   Q9JX32; A1INU6;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Putative zinc metalloprotease NMA0084;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=NMA0084;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AL157959; CAM07403.1; -; Genomic_DNA.
DR   PIR; C82000; C82000.
DR   RefSeq; WP_002239454.1; NC_003116.1.
DR   AlphaFoldDB; Q9JX32; -.
DR   SMR; Q9JX32; -.
DR   EnsemblBacteria; CAM07403; CAM07403; NMA0084.
DR   KEGG; nma:NMA0084; -.
DR   HOGENOM; CLU_025778_0_2_4; -.
DR   OMA; QYMVGFG; -.
DR   BioCyc; NMEN122587:NMA_RS00445-MON; -.
DR   Proteomes; UP000000626; 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; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 2.
DR   Pfam; PF17820; PDZ_6; 2.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..446
FT                   /note="Putative zinc metalloprotease NMA0084"
FT                   /id="PRO_0000088450"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          100..181
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   446 AA;  48022 MW;  F8C8B1109A8A38A4 CRC64;
     MHTLLAFIFA ILILVSLHEF GHYIVARLCG VKVVRFSVGF GKPFFTRKRG DTEWCLAPIP
     LGGYVKMVDT REGEVSEADL PYAFDKQHPA KRIAIVAAGP LTNLALAVLL YGLSFSFGVT
     ELRPYVGTVE PDTIAARAGF QSGDKIQSVN GTPVADWGSA QTEIVLNLEA GKVAVGVQTA
     SGAQTVRTID AAGTPEAGKI AKNQGYIGLM PFKITTVAGG VEKGSPAEKA GLKPGDRLTA
     ADGKPIASWQ EWANLTRQSP GKKITLTYER AGQTHTADIR PDTVEQPDHT LIGRVGLRPQ
     PDRAWDAQIR RSYRPSVVRA FGMGWEKTVS HSWTTLKFFG KLISGNASVS HISGPLTIAD
     IAGQSAELGL QSYLEFLALV SISLGVLNLL PVPVLDGGHL VFYTAEWIRG KPLGERVQNI
     GLRFGLALMM LMMAVAFFND VTRLLG