ID A0A2K9F7X8_9RHOB Unreviewed; 453 AA.
AC A0A2K9F7X8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:AUH35331.1};
GN ORFNames=CUV01_09070 {ECO:0000313|EMBL:AUH35331.1};
OS Paracoccus tegillarcae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1529068 {ECO:0000313|EMBL:AUH35331.1, ECO:0000313|Proteomes:UP000233742};
RN [1] {ECO:0000313|EMBL:AUH35331.1, ECO:0000313|Proteomes:UP000233742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM15 {ECO:0000313|EMBL:AUH35331.1,
RC ECO:0000313|Proteomes:UP000233742};
RA Hurst M.R.H.;
RL Submitted (DEC-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP025408; AUH35331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9F7X8; -.
DR KEGG; paro:CUV01_09070; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000233742; Chromosome.
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:UniProtKB-KW.
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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233742};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..453
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014992089"
FT DOMAIN 37..181
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..371
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 233..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49812 MW; 6BFE55FA927A8AC9 CRC64;
MRALTLTAAL AVLPAMSLAD MPDGISHFTL PNGLETVVIE DHRAPVVVQM VWYRIGAADE
QPGKSGIAHY LEHLMFKGTD KLAPGELSKT VIANGGKDNA FTSYDYTAYF QRIAADRLPL
IMEMEADRMA NLKIGPDDWQ AEREVVLEER AQRTDSEPSA LFAEERNAVQ FYNHPYGRPV
IGWRAEMMGL TREDAIDWYD SHYAPNNAIL ILAGDVTPER ARELADEFYG PIPAKEDLAE
RSRPQEPEQA SPRRMQRVDA RVPQPIMVRT AIATERNRGD QKSAAALTVL AELLGGSMQT
SVLGRKLALP GKALWVGAGY DGLAVDPTTF VLSMAPADDL LPEEAEALLD QVLADFLEEG
PDPDDLERVK TGIRASRIYA QDSAHGRAYD YGQGLSTGLS IEDVNDWPDI LADVTAEDVM
AAARDVLDSD ASVTGWLLPE QPAPENRQKE SQE
//
