ID   M5T4E1_9BACT            Unreviewed;       419 AA.
AC   M5T4E1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Processing peptidase {ECO:0000313|EMBL:EMI40336.1};
GN   ORFNames=RRSWK_07129 {ECO:0000313|EMBL:EMI40336.1};
OS   Rhodopirellula sp. SWK7.
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=595460 {ECO:0000313|EMBL:EMI40336.1, ECO:0000313|Proteomes:UP000012028};
RN   [1] {ECO:0000313|EMBL:EMI40336.1, ECO:0000313|Proteomes:UP000012028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWK7 {ECO:0000313|EMBL:EMI40336.1,
RC   ECO:0000313|Proteomes:UP000012028};
RX   PubMed=23273849;
RA   Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA   Achstetter T., Glockner F.O., Harder J.;
RT   "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT   sulfatases in the genus Rhodopirellula.";
RL   Mar. Genomics 0:0-0(2012).
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:EMI40336.1}.
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DR   EMBL; ANOQ01000138; EMI40336.1; -; Genomic_DNA.
DR   RefSeq; WP_009105358.1; NZ_ANOQ01000138.1.
DR   AlphaFoldDB; M5T4E1; -.
DR   STRING; 595460.RRSWK_07129; -.
DR   PATRIC; fig|595460.3.peg.7763; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000012028; 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          15..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..345
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   419 AA;  46220 MW;  9A60201302C7DB27 CRC64;
     MSDFRSVTLD NGLQVVAEVD NRGYSAAIGY FVRAGARDEN DSQSGLSHFL EHMMFKGTAT
     RSAAEVNREL DELGGQSNAY TSEEQTVYYA AVLPKYQRRM VDLLSDMMRP RLDADEFATE
     RGVILEEIAK YEDQPPFGAF ERVMECCYGP RGLGRRVLGT TESITNMHVD TMRDYFSARY
     RPANMVLAAS GNLDFDDLVE QAGEATAAWN DLPMPAAFAS DNKDVLPAGV ELNPRLAVPD
     ATQAYRVTLS GGPSMAASDR YAMRLLASIV GDDGGSRLFW DLIDTGRAEI ATLWPQEYSD
     TGALFSYLVC TPDQMDSNIR LMNEAIDLVV RDGVKQDELN QVINKTVAGV IMASERPSQR
     LFGLGSHWLC CREYLSTDEL LDAYRRVDVA AIGDAARNYL CCEPTEVIAS ASDEPSLTT
//