ID   Q82VB3_NITEU            Unreviewed;       814 AA.
AC   Q82VB3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Serine proteases, subtilase family {ECO:0000313|EMBL:CAD85094.1};
GN   OrderedLocusNames=NE1183 {ECO:0000313|EMBL:CAD85094.1};
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD85094.1, ECO:0000313|Proteomes:UP000001416};
RN   [1] {ECO:0000313|EMBL:CAD85094.1, ECO:0000313|Proteomes:UP000001416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC   {ECO:0000313|Proteomes:UP000001416};
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA   Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D., Hommes N.,
RA   Whittaker M., Arp D.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; AL954747; CAD85094.1; -; Genomic_DNA.
DR   RefSeq; WP_011111772.1; NC_004757.1.
DR   AlphaFoldDB; Q82VB3; -.
DR   STRING; 228410.NE1183; -.
DR   MEROPS; S08.A50; -.
DR   DNASU; 1082127; -.
DR   KEGG; neu:NE1183; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_018485_0_0_4; -.
DR   OrthoDB; 6306157at2; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07487; Peptidases_S8_1; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          491..800
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        499
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        545
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        755
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   814 AA;  89117 MW;  626C9CDEE128B6BE CRC64;
     MATEKRSSRS TSSKSSGSKS AGTGKTRQPG VEHISPFAQF SRSAASTKSA EFPSILNKEG
     SSPEVGTIVY IHGIGNKPVA SILKCQWDTA LFGAPMGDRT RMAYWVDRNR YPKPKDASCA
     DKDTLPEDAG GMGVQALQEN ELEPEIKLSA AERKIMAALE ERLRAGEKQP GGVNVKVLPL
     PESVRLWITR RITKLFLKDV QDFFFDEHKR NVMEQSLRDR LDVGGGPFIV VAHSQGSMIA
     YHVLRQLKKA DCDVRLFITI GSPLGIQEAQ DVLGKIGSGK PLAVPECVDR WLNVAERLDP
     VALDSDLGND YQPNSHGVKI ENHAGLMINP EWASNPHSGT GYLSLDIVRQ AVRETAGPTF
     SNPVGRNILM KDLVDNIEDG HREQRHPTLI QLVSDDDDAT SLDEVRDRLS NLIKNVLIFN
     NAEPEEGRIQ LMRRFISADL TRSEIEELRS HCSTLKIDRV WRNALKRTLL HQSAHTIQVR
     PANLGYGACG QNIAWAVLDT GIAADHPHFK KHNNVVAQWD CTGSGSPREL RLGDSGFGTL
     DGHGHGTHVA AIIAGTLTLP HDEKDKSEIL LQGMAPEARL YGFKVLKDNG NGEDAFIIKA
     LDTIAELNER AGKLVIHGVN LSLGGNFDPS VFGCGHTPLC QELRRLWRQG VLVCLAAGNE
     GYALLDSASG VIPANMDLSI GDPANLEEAI SVGSVHKTNP HTYGISYFSS RGPTADGRMK
     PDLVAPGENI LSARHQWPKS KLTMRNAYVE MSGTSMATPH VSGLFAAFLS ARREFIGYPD
     RVKTLLLQHC TDLARDPYIQ GKGMPNLVRM IMNT
//