ID   F9ZG92_9PROT            Unreviewed;      1639 AA.
AC   F9ZG92;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Peroxidase/Serralysin {ECO:0000313|EMBL:ADZ27123.1};
DE            EC=1.11.1.7 {ECO:0000313|EMBL:ADZ27123.1};
DE            EC=3.4.24.40 {ECO:0000313|EMBL:ADZ27123.1};
GN   ORFNames=NAL212_2301 {ECO:0000313|EMBL:ADZ27123.1};
OS   Nitrosomonas sp. AL212.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=153948 {ECO:0000313|EMBL:ADZ27123.1, ECO:0000313|Proteomes:UP000001629};
RN   [1] {ECO:0000313|EMBL:ADZ27123.1, ECO:0000313|Proteomes:UP000001629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL212 {ECO:0000313|EMBL:ADZ27123.1,
RC   ECO:0000313|Proteomes:UP000001629};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y., Klotz M.G.,
RA   Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.;
RT   "Complete sequence of chromosome of Nitrosomonas sp. AL212.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP002552; ADZ27123.1; -; Genomic_DNA.
DR   STRING; 153948.NAL212_2301; -.
DR   KEGG; nit:NAL212_2301; -.
DR   eggNOG; COG2931; Bacteria.
DR   HOGENOM; CLU_000493_0_0_4; -.
DR   Proteomes; UP000001629; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09821; An_peroxidase_bacterial_2; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR013858; Peptidase_M10B_C.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   PANTHER; PTHR11475:SF4; LD42267P; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00353; HemolysinCabind; 8.
DR   Pfam; PF08548; Peptidase_M10_C; 1.
DR   PRINTS; PR00313; CABNDNGRPT.
DR   SUPFAM; SSF51120; beta-Roll; 4.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ADZ27123.1};
KW   Oxidoreductase {ECO:0000313|EMBL:ADZ27123.1};
KW   Peroxidase {ECO:0000313|EMBL:ADZ27123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001629}.
FT   DOMAIN          1521..1628
FT                   /note="Peptidase M10 serralysin C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08548"
FT   REGION          410..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1639 AA;  172318 MW;  021064B14D2E4D18 CRC64;
     MANFSRTDLD FLLQQIAIAD ADSAAQQQPN PIFNALPGLV GDPLLPFGLR NVDGTYNNLE
     DGQSLFGSAD QVFPRGLSIF LRPGEQITFD PDGPGPQTVG QSTHYNQTKG AVFDSQPRTV
     SNLISDQTAT NPAAIAVANG TPGSELVNGT RADGSAFQTY FIPNVTPDAG LSAPYNSWFT
     FFGQFFDHGL DLVNKGQSGT VFVPLLDDDP LVTGPDGILG DDPLTVGVDE SLDDLPEGLR
     FMALTRATNK PGNDGIMGTG DDVRDHVNQT TPFVDQNQTY TSHPSHQVFL REYELNGAGR
     PVSTGNLLED STTGDGLATW ADIKAQAQNM LGINLTDADL TNLPLLATDT YGKFIPGSNG
     FVQIVTSSGL VQGNPAANGG NGIDIPGNAV RTGHAFLDDI AHTAVPKFAS GLLNPDPDPD
     TGNTPAPGTY DDELLDAHFI TGDGRGNENI GLTTVHTVFH AEHNRKVQEI KQLITASGDT
     PFMNQWKLPN GNWDGDKLFQ AARFATEMQY QHLVFEEFAR KVQPNVDVFI GYDSSIDPAI
     MAEFAHVVYR FGHSMLTEKV ERIDAQGDSN DIGLIQAFLN PVEFGADYAN NSEAAAAVVR
     GMTKQVGNEV DEFVTEALRN NLLGLPLDLP TINITRGRDT GMPGLNDARR MFFDDVGHPS
     LAPYESWNDF KLDLKNPESL TNFIAAYGNH PSINSVTTME DKRAAADLLV KGGPGAPADR
     ANFMNSTGAY TTANSGLDSV DFWIGGMAEK QAPFGGLLGS TFNYVFETQM ENLQNGDRFY
     YLARTAGMDF LTQLEENSFA EMIMRNLPDV KHLPFDVFST PTYIFEASAQ TVSGTIIDDP
     DTTTYDERDL LIRDTSLGPD TIRYTGEDHV VMGGTESNDR LRAGAGDDTL WGDGGNDRLE
     GGAGNDSING GDGNDRITDA SGDDNIKGGD GHDFINGGAG INLILAGSGH DFVVTGNDIS
     EVFAGPGNDF IFGNAPNEVM QGNEGDDWIQ TGTADGSTGD NFDPFNRDPI RGNDVFVGSG
     GLDEFIGEGG DEVMMGLAGA DRNDGGSGFD WTANVGSTVA ANVDLARLLV PGPFVDTADR
     FDLVEAASGW NQNDTIRGDD RTSTELELID PNTGQNNALD NVNQLNGTHT VAERIGMISG
     LSALLDNPTT PQNEGTSFSA GNILLGGGGS DLIEGRGGDD IIDGDAWLNV RILAGTQSFP
     NMTPALRTAM QNGTYSPDQL VIVREILSNS TGVDTALYGD VFANYVVNVD STGTIFVDHA
     NPVVGDDGSD RIRNVERLQF ADRIVTVGTN GDDNMVGTAG NDVLLALGGN DTLDGLDGVD
     ILNGGPGDDT YTVNTTTDTI IELAGVGSGI DTVASSVTYT LGLNLENLTL TGTAPNGTGN
     NVGNVITGNA SNNILTGLGG DDTLIAGGGT DTLRGGLNND TYVISNLPVT ITELLNQGTD
     TVESPVTYTL LANVENLTLT GGDAINGTGN GLANILTGNS NNNTLNGGAG LDTLNGGDGN
     DTLNGAAGID ILNGDNGADT LIGGPSADTL IGGAGADIFD YLAAVGHSNP ANRDTIMDFE
     TGIDTIDLSA IDANVLAAFP GNQAFIFIGS DAFSGGGQLR YDSATGLLQA NINANAAAEF
     EIQLFGSPTP TLAVGDLVL
//