ID A0A258GZT9_9PROT Unreviewed; 983 AA.
AC A0A258GZT9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=B7Y90_06450 {ECO:0000313|EMBL:OYX49512.1};
OS Alphaproteobacteria bacterium 32-64-14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1970492 {ECO:0000313|EMBL:OYX49512.1, ECO:0000313|Proteomes:UP000215897};
RN [1] {ECO:0000313|EMBL:OYX49512.1, ECO:0000313|Proteomes:UP000215897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-64-14 {ECO:0000313|EMBL:OYX49512.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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}.
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:OYX49512.1}.
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; NCEM01000013; OYX49512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258GZT9; -.
DR Proteomes; UP000215897; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 123..259
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 277..448
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 559..670
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 711..888
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 983 AA; 106553 MW; A6DC882BBDB3F254 CRC64;
MRKAPNACAR GSASRSEVRR FESYCFSICA AYSALTQFKG STMFRSRTTL KFGAATIALL
TASACATSGP TSDTYAAPMI PAAAPEQAAA PARDPVVAEI SAMKFDIPYT KYVLQNGLTL
IVHEDTKTPT VTAHLIYHVG SKNEPKGRSG FAHLFEHLMF NGSEHFNDDF FKATQQFGAT
NQNGSTNTDR TNYYQTVPKE ALDSILWLES DRMGFLLGAV DQARLDEQRG VVQNEKRQGE
NQPYGQVFNH IIAATYPEHH PYGHTVIGSM EDLEAASLKD VQDFFKTWYG PSNAILVLAG
DIKPEEAKAK VEKFFGEIPP GPPPSQAKSW VPELAPNQRE ILYDRVAQPR IYITWNVPEL
GNADGEQLDH VAAALGGDRN ARLTKRLVHD EQVATSVSVG NPQSEIAGQF RIVVTAKPDA
DLAKIEAAIN EELRRIIASG PTQAEIDKNI VQTVSGIISG LESTSDKAAQ LAQWEMIAGE
PSGWKGSLER LEAATPATVQ AAAAKWLTRG AYTLTVLPFG SPKAFSAAVD RSKMPAPGAV
SDTVFPAYQT ATLSNGVKVY LVERHDVPEV TLYTQFDTGY PADQSTIKEG LGSLTANLMD
EGTTSRTALQ IADEIDRLGA SLGTSGGGEQ AAVSFSALTP TLDRVMAIWT DVMRNPAFTA
GDFQRIQAQT VQGLQQQLRD PASIGQRVMS RALWGDAHPY GRLVDPQDIT SLTAADAAAF
HKAWYGPNNA TIFIVGDTTL AQITPKLEAA FAGWANAPNK SAPVANGVRP TKPIVYIVDR
PDSVQSTILV ATPQPPRNPA DDTRVSAFNA LFGGNFTSRV NMNLREDKGW SYGARSQVSG
GRGPRTFMIS APVQTDQTKG AIAELRKELT EVVGRRPPNA AELDTVRTNT LLGMASRWET
SGAVLNSLVD IHQFNLPADY WSNYADTYRS ATSTDIAAMA KRIIPDQNHI WVIVGDRAKI
EQGIRELNLG EIRVVDENGN PVQ
//
