ID A0A0P8C2Z5_9RHOB Unreviewed; 454 AA.
AC A0A0P8C2Z5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KPQ16932.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:KPQ16932.1};
GN Name=pqqL {ECO:0000313|EMBL:KPQ16932.1};
GN ORFNames=HLUCCO18_06755 {ECO:0000313|EMBL:KPQ16932.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ16932.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ16932.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ16932.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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:KPQ16932.1}.
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; LJSY01000012; KPQ16932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8C2Z5; -.
DR STRING; 1666917.HLUCCO18_06755; -.
DR PATRIC; fig|1666917.4.peg.193; -.
DR Proteomes; UP000050333; Unassembled WGS sequence.
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, ECO:0000313|EMBL:KPQ16932.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KPQ16932.1};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..454
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006148677"
FT DOMAIN 38..183
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 454 AA; 50483 MW; 7BA912DFF5423208 CRC64;
MLRRIALTLV ATLTVALTST VQAAENVTEF FLENGMQVVV IEDHRSPAVV HMVWYRAGAA
DEPPGASGVA HFLEHLMFKG TDELESGEFS RIVEANGGTD NAFTSWDYTG YIQRVAADRL
GLLMEMEADR MRDLRFADEE VVTERSVIIE ERAERVDSSA GGLFNEQMRA TLFNNHPYGI
PIIGWRHEMQ ELDRAALIAF YDAHYWPNNA VLIVAGDVTP DEVRRLAQEH YGPIPANPDI
TARARPQEPP QIADRRVIYE DERVANPYVA RTYLTPAREP GDQRRAAALT MLAEILGGSG
QTSVLARQLQ VEEERALYAA AFYDATSYDP SSFNIVNVPV PGVPLEEAEA DLDRTIAEFL
ENGIDPAQFE RIKFQIEAAQ IYEEDNVQGL ARSYGVALTS GLTVEDVDTW PDVLAAVTID
EVMEEARRLF SETRSVTGYL MQPAPESAAD EVTQ
//
