ID   A0A1W9KRX8_9BURK        Unreviewed;       468 AA.
AC   A0A1W9KRX8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OQW87081.1};
GN   ORFNames=BWK72_14785 {ECO:0000313|EMBL:OQW87081.1};
OS   Rhodoferax ferrireducens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=192843 {ECO:0000313|EMBL:OQW87081.1, ECO:0000313|Proteomes:UP000192505};
RN   [1] {ECO:0000313|EMBL:OQW87081.1, ECO:0000313|Proteomes:UP000192505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A7 {ECO:0000313|EMBL:OQW87081.1};
RA   Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA   Ruberg S.A., Marcus D.N., Dick G.J.;
RT   "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT   chemosynthetic microbial mats in the Lake Huron basin.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OQW87081.1}.
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DR   EMBL; MTEI01000011; OQW87081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9KRX8; -.
DR   Proteomes; UP000192505; 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; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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          50..189
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          198..383
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  51432 MW;  EA7E25EC92561853 CRC64;
     MAALLLTTPP LTQAQPAPPA SPASAVAVAP ESAQQFTLAN GLTLIVKPDR RAPTAVHMLW
     VRVGAMDEVD GASGVAHVLE HMMFKGTPKV PAGEFSRRVA ALGGRDNAFT SRDYTGYYQM
     VPVQKLEDVM RLESDRFAHS QWPDAEFKKE LEVVKEERRL RTEDNPQALM YEALNATVFV
     ASPYRRPIVG WMSDLEALTP EDARAFYQRW YVPANAAVVV AGDVDVAQVR ALADKYYGSL
     PTRAVPERKP RTEPVQSGLK RLAFKAPAEQ ANVVLAYKVP SLKWQVGSAN DADTLALTVL
     AAVLDGYQGA RLERSLTQGP DRVADSAGAY NGLWGRGPQL FMLTGVPTQG KTAEQVEQAL
     RTQVQRIATE GITEAELARV KTQWVASEVY KLDSLFNQAR ELGTQWAQGL PTDAGDQLLQ
     RLRAVTAEQV QQVARQYFGD DQLTVAHLLP QPLDKTRKPR TPPAGFRH
//