ID   Y183_NEIMB              Reviewed;         446 AA.
AC   Q9K1G9;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative zinc metalloprotease NMB0183;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=NMB0183;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF40640.1; -; Genomic_DNA.
DR   PIR; H81228; H81228.
DR   RefSeq; NP_273241.1; NC_003112.2.
DR   RefSeq; WP_002243948.1; NC_003112.2.
DR   AlphaFoldDB; Q9K1G9; -.
DR   SMR; Q9K1G9; -.
DR   STRING; 122586.NMB0183; -.
DR   PaxDb; Q9K1G9; -.
DR   EnsemblBacteria; AAF40640; AAF40640; NMB0183.
DR   KEGG; nme:NMB0183; -.
DR   PATRIC; fig|122586.8.peg.225; -.
DR   HOGENOM; CLU_025778_0_2_4; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000425; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..446
FT                   /note="Putative zinc metalloprotease NMB0183"
FT                   /id="PRO_0000088451"
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;  48024 MW;  A32AB9349C58752B 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 GKKITLNYER AGQTHTADIR PDTVEQSDHT LIGRVGLRPQ
     PDRAWDAQIR RSYRPSVVRA FGMGWEKTVS HSWTTLKFFG KLISGNASVS HISGPLTIAD
     IAGQSAELGL QSYLEFLALV SISLGVLNLL PVPVLDGGHL VFYTAEWIRG KPLGERVQNI
     GLRFGLALMM LMMAVAFFND VTRLLG