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Database: UniProt
Entry: A0A1H7ZWR3_9RHOB
LinkDB: A0A1H7ZWR3_9RHOB
Original site: A0A1H7ZWR3_9RHOB 
ID   A0A1H7ZWR3_9RHOB        Unreviewed;       466 AA.
AC   A0A1H7ZWR3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:SEM61737.1};
GN   ORFNames=SAMN04488003_102129 {ECO:0000313|EMBL:SEM61737.1};
OS   Loktanella fryxellensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=245187 {ECO:0000313|EMBL:SEM61737.1, ECO:0000313|Proteomes:UP000199585};
RN   [1] {ECO:0000313|EMBL:SEM61737.1, ECO:0000313|Proteomes:UP000199585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16213 {ECO:0000313|EMBL:SEM61737.1,
RC   ECO:0000313|Proteomes:UP000199585};
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}.
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DR   EMBL; FOCI01000002; SEM61737.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7ZWR3; -.
DR   STRING; 245187.SAMN04488003_102129; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000199585; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SEM61737.1};
KW   Protease {ECO:0000313|EMBL:SEM61737.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199585};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..466
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011662996"
FT   DOMAIN          36..179
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          186..360
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          427..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  49355 MW;  E678BDB722CD3691 CRC64;
     MIRILTLCLT LVAGTAHAAV EIEEVTSPGG IEAWLVEDHN IPFTALEIRI VGGAALDAPG
     KRGATNLMMA LLEEGADDLT AQAFQTRREE LAASYGFDAD DDMVAISAQM LTENRDEAVA
     LLRSALVAPR FDQDAVDRVR AQVLANIASD EKSPGDIASR ALDAAAFGDH PYGASLSGTV
     ESVTALTRDD IVVAHRATLT RDRVYVGAVG DITPEDLGAL LDDLLGDLPA ATVPLPDDAD
     YALTGGVTVI PYDTPQSVAL FGHRGITRDD PDYMAAYILN EALGAGGFES RLMQEVREER
     GLTYGISTFL VPQFYGELIL GQLGSSNSTM AEAIDVIRAE WARMATDGMT QEELDRVKTY
     LTGAYPLRFD GNASIATILV GMQVIDLPPS YVVDRNAQLN AVTLDDVNRV ARELLRPDDL
     RFVVVGQPEG LTGDPAPGGV LPQDAAPAPE TAPADAAPTE AAPAAD
//
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