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Database: UniProt
Entry: A0A0D7EFM6_RHOPL
LinkDB: A0A0D7EFM6_RHOPL
Original site: A0A0D7EFM6_RHOPL 
ID   A0A0D7EFM6_RHOPL        Unreviewed;       429 AA.
AC   A0A0D7EFM6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KIZ39543.1};
GN   ORFNames=OO17_20145 {ECO:0000313|EMBL:KIZ39543.1};
OS   Rhodopseudomonas palustris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ39543.1, ECO:0000313|Proteomes:UP000032515};
RN   [1] {ECO:0000313|EMBL:KIZ39543.1, ECO:0000313|Proteomes:UP000032515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL398 {ECO:0000313|EMBL:KIZ39543.1,
RC   ECO:0000313|Proteomes:UP000032515};
RA   Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT   "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT   isolated from estuarine surface water.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIZ39543.1}.
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DR   EMBL; JXXE01000421; KIZ39543.1; -; Genomic_DNA.
DR   RefSeq; WP_044414844.1; NZ_JXXE01000421.1.
DR   AlphaFoldDB; A0A0D7EFM6; -.
DR   STRING; 1421013.GCA_000504425_03439; -.
DR   PATRIC; fig|1076.23.peg.4664; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000032515; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 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;
FT   DOMAIN          14..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   429 AA;  46412 MW;  F9AE24ED68E711D2 CRC64;
     MSVELTKLPS GLTVVTDTMP HLETAALGVW TGVGGRDEKA DEHGISHLLE HMAFKGTKRR
     SSREIAEEIE AVGGDLNAGT STESTAYYAR VMKADVPLAL DVLSDILANP SFDPEELERE
     KSVIVQEIGA AQDTPDDMVF EYLNELCYPE QPIGRSLLGT PQTLKTFDRA TLQNYLSTHY
     RGPEMVVAAA GAVDHQQVVA EVERRFASFD GSVAPKPEPA MFGNGGSRVV HRDLEQAHLT
     LALEGLPQSD PSLFSLQVFT NVLGGGMSSR LFQEVREKRG LCYSIYTFHA PYSDTGFFGL
     YTGTDPVDAP EMMEVIVDVI NDAVETLTEA EIARAKAQMK AGLLMALESC SSRAEQLARH
     ILAYGRPLSV PELVAKIDAV SVETARDAAR GLLSRGRPAV VALGSGRELD SAVGFAEGLT
     QLRTKASYH
//
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