ID   I4VQW2_9GAMM            Unreviewed;       957 AA.
AC   I4VQW2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:EIL89603.1};
GN   ORFNames=UU5_15568 {ECO:0000313|EMBL:EIL89603.1};
OS   Rhodanobacter sp. 115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL89603.1, ECO:0000313|Proteomes:UP000004557};
RN   [1] {ECO:0000313|EMBL:EIL89603.1, ECO:0000313|Proteomes:UP000004557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=115 {ECO:0000313|EMBL:EIL89603.1,
RC   ECO:0000313|Proteomes:UP000004557};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:EIL89603.1}.
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DR   EMBL; AJXS01000372; EIL89603.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4VQW2; -.
DR   PATRIC; fig|1162282.3.peg.2938; -.
DR   Proteomes; UP000004557; 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; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF21; PROCESSING PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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:EIL89603.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          43..183
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          201..375
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          519..639
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          673..852
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   957 AA;  103511 MW;  8DAA5B53BFE562C1 CRC64;
     MLTLGAGALP VMAAPAAAAG DAAQAALPDI PYTRFVLPNG LTVVVSEDHK APVVAVAMWY
     HVGSAREPTG KSGYAHLFEH LMFERSGHHD GNYFQPFEKV GATGMNGTTA NDRTNYFETV
     PTTALDMALW MESDRMGWLL DGLGQDEVNQ QRGVVQNEKR QDENQPYGLR VQENIEANAY
     PLNHPYHHDT IGSMKDLNAA SIDDFKTWFR TYYGAANATL VMVGDITPAE AKAKALKYFG
     EIPSGPPVAK LQPWTFPRST STRGTMHMDV PQVHIYREWN TPHGGTEADN LLSLAATVLG
     DGKTSRLYQR LVYQDKLADD VSVSQNSGEL ASQFELEVDV KNGVDPAKVE AAVADVWKTF
     LKDGPTADEL ARAKTGFRAG YVRRLEKVGG FSGKATLLAA GQVYHDDPGA WRKDLAAMMA
     ATPAQVRDAA RKWISKGDYT LTVLPLAKGQ QASTADVAET GGLGTAPGAP KPVPAAKHDW
     HTVKSDVDRS KGVPEVTTFP DLKFPTLEHA KLANGIEVTL AERHDVPLVQ MELLFDAGYA
     ADQGRKLGTS SFTMYMLNEG TEDLDSVQIA KRKQRLGSYI NTGCGLDYCN ISMNALTDKV
     VPSLKLVADV ARNPAFRASD IARLRGQWLA GIEQEKARPI TMALRVLPPL LYGKGHAYAI
     PFTGSGTTAS IKSLTAADMR NFMGDYIRPD NVKILVAGDT TLAKLVPELN AVFGNWKAPA
     NAVPKKNIAK VNYPGHVRVF LMDRPGSLQS VILAGEVAPS TEAPNNLEIG TMNGAFGGSF
     TSRLNMNLRE GKHWAYGAFS FLQNAVGQRP FMIYAPVQTD KTAPSISEAL KEAKAIVGPK
     PLTDAEIQKI KDNDVRAMPG EYQTVSAVLG AMQGIALYHR PDDYVQTLKS RIESQSDKAV
     QAAADEVIKP DELTWVIVGD LKKIGPSVRA LQLGSVQVLD TDGKPVAAKD GGATNEK
//