ID   Y1322_FUSNN             Reviewed;         339 AA.
AC   P58819;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Putative zinc metalloprotease FN1322;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=FN1322;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009951; AAL95518.1; -; Genomic_DNA.
DR   RefSeq; NP_604219.1; NC_003454.1.
DR   AlphaFoldDB; P58819; -.
DR   SMR; P58819; -.
DR   STRING; 190304.FN1322; -.
DR   EnsemblBacteria; AAL95518; AAL95518; FN1322.
DR   KEGG; fnu:FN1322; -.
DR   PATRIC; fig|190304.8.peg.1886; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_0; -.
DR   InParanoid; P58819; -.
DR   OMA; QYMVGFG; -.
DR   BioCyc; FNUC190304:G1FZS-1897-MON; -.
DR   Proteomes; UP000002521; 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; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 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..339
FT                   /note="Putative zinc metalloprotease FN1322"
FT                   /id="PRO_0000088441"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..179
FT                   /note="PDZ"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   339 AA;  37614 MW;  34EB5AA861834A83 CRC64;
     MTFLIAVVML GLIIFVHELG HFLTAKLFKM PVSEFSIGMG PQVFSVDTKK TTYSFRAIPI
     GGYVNIEGME VGSEVENGFS SKPAYQRFIV LFAGVFMNFL MAFILLFVTA KISGRIEYDT
     NAIIGGLVKG GANEQILKVD DKILELDGKK INIWTDISKV TKELQDKEEI TALVERNGKE
     ENLTLKLTKD EENNRVVLGI SPKYKKIDLS TTESLDFAKN SFNSILIDTV KGFFTIFSGK
     VSLKEVSGPV GIFKVVGEVS KFGWISIASL CVVLSINIGV LNLLPIPALD GGRIIFVLLE
     LVGIKVNKKW EKKLHKGGMI LLLFFILMIS VNDVWKLFN