ID   A0A099G9R4_9RHOB        Unreviewed;       421 AA.
AC   A0A099G9R4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KGJ19565.1};
GN   ORFNames=IX56_15910 {ECO:0000313|EMBL:KGJ19565.1};
OS   Paracoccus sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ19565.1, ECO:0000313|Proteomes:UP000029858};
RN   [1] {ECO:0000313|EMBL:KGJ19565.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ19565.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ19565.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ19565.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-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:KGJ19565.1}.
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DR   EMBL; JRKQ01000127; KGJ19565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099G9R4; -.
DR   Proteomes; UP000029858; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029858}.
FT   DOMAIN          15..161
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          168..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   421 AA;  45503 MW;  95BD7A0FE1CC3F14 CRC64;
     MSDIRITTLT NGLRIATRRM EGLHSASVGV WVTAGGRDER AEQNGIAHFL EHMAFKGTAR
     RTALQIAEAI EDVGGYINAY TSRDTTAYYA RVLAGDVPLA LDVLGDIVLN PAFDGREIEV
     ERGVILQEIG QSLDTPDDVI FDWLQEAAYP GQAMGRTILG PAERVSGFSR DDLAGFVREH
     YGPGQMIVAA AGAVDHDTLA RQAEEIFGHL APVTDPGREP ARWQGTEARR VKRLEQAHFA
     LAFEGPGYLA PDFYAAQIWT SALGGGMSSR LFQRIREERG LCYTIFAQSG FHDDTGMVTV
     YAGTSGEQLA DLAHLTIDEI RRSADEMTEA EVARAKAQLK AGLLMGLESP SGQAERIARA
     LAIWGRVPDA EEVAQRIDAV TAAEVRDHAA GLIAAARPAL ALYGPVRRGP SREALAERLA
     A
//