ID F8GH72_NITSI Unreviewed; 467 AA.
AC F8GH72;
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 M16 domain protein {ECO:0000313|EMBL:AEJ00238.1};
GN OrderedLocusNames=Nit79A3_0350 {ECO:0000313|EMBL:AEJ00238.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ00238.1};
RN [1] {ECO:0000313|EMBL:AEJ00238.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ00238.1};
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 -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP002876; AEJ00238.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GH72; -.
DR STRING; 261292.Nit79A3_0350; -.
DR MEROPS; M16.019; -.
DR KEGG; nii:Nit79A3_0350; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_4; -.
DR OrthoDB; 9811314at2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003371604"
FT DOMAIN 47..190
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..383
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 467 AA; 52869 MW; 408949530CCFDF75 CRC64;
MKPDHRTNLF RYFSFSRLLL LSSLLISLPT FANPHEYILD NGLKLIVKQD HRSPVVVSQI
WYKTGSIDEL NGVTGVAHVL EHMMFKGTEK VPNGEFSKKI AAAGGRENAF TSYDYTGYYQ
QLHKRSLPMA MELESDRMRN LILTEEEFAK EIKVVMEERR LRTDDQARAL LYEKMMAMAY
QSHPYKNPII GWMNDLENMR VEDAQEWYDR WYAPNNAILV VVGDVDAEEV FKLAQKNYGL
IQKRPLLPID ARKPQTEPPQ VGTKRITVKA PAELPYLIMG YHAPTIRNVT ADWEPYALEI
LEGVLDGNAS ARLNKSLVRE NQVANSASAG YGAMARGPGI FFLSAVPRAG KTVVELEQAL
RGEIEKIIKE GVTEEELARV KAQVVASHVY QRDSIYSQAM QLGRLESMGL SFRDIDTILE
KLKAVTAEQI RDVTKKYFND DSLTVAVLDP QPLEKKLPAK APAGLRH
//
