ID A0A1I1HVG5_9RHOB Unreviewed; 472 AA.
AC A0A1I1HVG5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:SFC28057.1};
GN ORFNames=SAMN05421762_0402 {ECO:0000313|EMBL:SFC28057.1};
OS Pseudooceanicola nitratireducens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=517719 {ECO:0000313|EMBL:SFC28057.1, ECO:0000313|Proteomes:UP000231644};
RN [1] {ECO:0000313|EMBL:SFC28057.1, ECO:0000313|Proteomes:UP000231644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29619 {ECO:0000313|EMBL:SFC28057.1,
RC ECO:0000313|Proteomes:UP000231644};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOLX01000001; SFC28057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1HVG5; -.
DR STRING; 517719.SAMN05421762_0402; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000231644; 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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFC28057.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231644};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014191173"
FT DOMAIN 42..186
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 196..378
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 441..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 52146 MW; 35197B71B93D8C08 CRC64;
MRLKILSRLA AAVILAAPMM TTSAQASNDL VTDFELDNGM QVVVIEDHRA PVVVHMVWYR
AGAADETPGV SGVAHFLEHL LFKGTDTMEP GELSKTVAEN GGTDNAFTSH DYTAYFQRVA
ADRLGLMMTM EADRMKNVRL TEADILTERE VIIEERNQRT ENSPQALFRE QTMAAQYLNH
RYGVPVIGWR HEMETLDLDD ALSYYRTFYS PNNAILIVAG DVTPDEVRAL AQDHYGPIPA
NPDLPERIRP SEPAQTAERR MIYRDPRVAQ PYVTRSYLAP ERDPGDQDTA AALVMLSELL
GGGQTGYLTQ KLVFEQQVAL YTSAYYGGLS LDDTTFGTYI VPAEGVPLEE AEAALDAALA
QFIADGVDAE QLDRIKMQVR ASQIYERDNV EALARRYGAA MTQGLTIADI QAWPEILQEV
TEAEILTAAR EVLNRNRAVT GYLMGPEPQP EPQPEPAASP APATQAEPEV SQ
//
