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
//