ID V9WPJ7_9RHOB Unreviewed; 474 AA.
AC V9WPJ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Zn-dependent peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Gal_03343 {ECO:0000313|EMBL:AHD11062.1};
OS Phaeobacter gallaeciensis DSM 26640.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD11062.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD11062.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD11062.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) 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; CP006966; AHD11062.1; -; Genomic_DNA.
DR RefSeq; WP_024098668.1; NZ_AOQA01000011.1.
DR AlphaFoldDB; V9WPJ7; -.
DR MEROPS; M16.019; -.
DR GeneID; 31847697; -.
DR KEGG; pgd:Gal_03343; -.
DR PATRIC; fig|1423144.3.peg.3348; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_5; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000018782; 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:UP000018782};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..474
FT /note="Zn-dependent peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004783343"
FT DOMAIN 65..210
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 220..402
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 474 AA; 52541 MW; E28D673475BB8AC1 CRC64;
MIPPLKPMIR RVTGAAAFVA AMMAMEASGF SAGTFVRSAQ AQDATTQSDA NDLVSSFVLD
NGMQVVVIED HRAPVVQHMV WYRAGSADEP VGQSGVAHFL EHLLFKATDT LEAGELSATV
AANGGRDNAF TSYDYTAYFQ RVAADRLGLM MQMESDRMVN IRLTEQDIET EREVILEERN
QRTDSEPRAL FREQLNAAQY LNHRYGQPII GWRHEMEELD MADALSFYGT YYAPNNAILV
VSGDVDPGEV RRLAEETYGK IPANPDLPER LRSKEPPQTA ARRIVFKDAR VAQPFVQRSY
LAPERDSGAQ ERAAALYLLA ELLGGGSTSY LTNALQFDQQ VAVYTGVFYS DVSLDDTTFD
FLVVPGADVS LEEAEAALDA TFARFLEEGV DEAQLERIKL QLRAAEIYAR DNVDGIANRY
GRALASGLTV EDVQAWPRIL QSITADEIIA VAREVLRPEV SVTGWMMRDE EVSQ
//
