ID   F8GJX9_NITSI            Unreviewed;       503 AA.
AC   F8GJX9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:AEJ01688.1};
GN   OrderedLocusNames=Nit79A3_1890 {ECO:0000313|EMBL:AEJ01688.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01688.1};
RN   [1] {ECO:0000313|EMBL:AEJ01688.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01688.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA   Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP002876; AEJ01688.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8GJX9; -.
DR   STRING; 261292.Nit79A3_1890; -.
DR   KEGG; nii:Nit79A3_1890; -.
DR   eggNOG; COG4783; Bacteria.
DR   HOGENOM; CLU_030556_1_1_4; -.
DR   OrthoDB; 9810445at2; -.
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   CDD; cd07333; M48C_bepA_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..503
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005678444"
FT   DOMAIN          65..252
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   503 AA;  56141 MW;  0B4DDE1D3312E5EE CRC64;
     MKLICLIIAL SILFPANSYA HELPDLGDVS QATITPYQER QIGLQIMRQI RADPSYLDDP
     EIASYLSNLG HKLIANSEET NAGQSFEFFA LQDSSINAFA LPGGFMGFNS GLIIAAQSES
     ELAAVMSHEI AHVTQKHLAR MIAGQKFDLI KSLATLAVAI IAARSNPQAS QAILVASQAS
     AIQSKLDFTR KHEKEADRIG LNILLDAGFE PQGMSTFFER LQRAGRFHEN GAPSYLRTHP
     ITYERIADIQ NRIREMPYRQ VPDSIDFLLV RAKLRAMQGK PHDTVVQFKS RLDEKRYINE
     AVERYGYIHA LLRDKKNIQA SNELAHLYQI LQNDSSTSVL TNHPLGKTVR VENKNVIAGA
     MIETLSASVK LANGKITEAF DIYKTALRIY PQHRALIHGY AHALLQNKLT ETALEFINKQ
     LLLIPNDPQL FSLQAQCYAL LGDRMLEHRA LAESYALKGH IAAALDQLQT ALQNSNGNFY
     QLSSVEARLK QIQALKAEED KEK
//