ID A0A2G5L4J1_9BACT Unreviewed; 940 AA.
AC A0A2G5L4J1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BFP72_14590 {ECO:0000313|EMBL:PIB36539.1};
OS Reichenbachiella sp. 5M10.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Reichenbachiellaceae;
OC Reichenbachiella.
OX NCBI_TaxID=1889772 {ECO:0000313|EMBL:PIB36539.1, ECO:0000313|Proteomes:UP000229466};
RN [1] {ECO:0000313|EMBL:PIB36539.1, ECO:0000313|Proteomes:UP000229466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5M10 {ECO:0000313|EMBL:PIB36539.1,
RC ECO:0000313|Proteomes:UP000229466};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Reichenbachiella sp. strain 5M10.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:PIB36539.1}.
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; MDGR01000007; PIB36539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5L4J1; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000229466; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase 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:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000229466};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..940
FT /note="Peptidase M16"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013619910"
FT DOMAIN 54..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 211..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 691..868
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 940 AA; 106650 MW; 8D4131F70E810C25 CRC64;
MKVFSSMKCH ALLLAMMLCF GSVLAQEPTE QLIPFDPSVR MGTLENGLTY YIKQNTKPEN
RVELRLVVNA GSILEDDDQQ GLAHFTEHMA FNGSKHFGKN DLVSYLQSVG VKFGAHLNAY
TSFDETVYIL PIPSDDEEIL ESGLTILEDW AGNLNFAQEE IDKERGVVIE EWRLGQGAQT
RMLQEYLPVI FKGSKYAERL PIGKKEILET FDRKTIVRYY EDWYRPDLMA VVAVGDIDVD
KMEERIKTHF SGLRNPDKQR QREEFDLPKN KEPLIAIASD PEATNILFNI MYKSEAQEFK
TLEQFRKSYV QALFLEMMNQ RLSDLLQSAN PPYLYAGTYI GSPVSRKTTA FSGYSVTKPD
DIKSGIVTLL EEIRRVELHG FNASELHTAK LNTLEAYESA YKERDKSKSE SLADELIRHF
LEHEPVPGIT FEYEFLKENI EGITIEEINS IIGNWIKAEN RVLYITAPEL EGLTLPTKEE
ILAWVAEIEQ KQMDPLAEVA VDTDLVKELP EGGKVTKVST YDRIEVKVLE LSNGATVYLK
PTDYKNDEIL FSAYRSGGIS VASDEDYWSA SFASSIISLS GVGDYSYTQL QKALAGKSLG
VSPYLSDLES GFSGNASPKD LETMLQLVFL YFTQVRTDEE AFQSLMQRNK AVLANVLSNP
NYYFQDRMAR IMSQGHLRGG GVPSVEDLEK VDRDAAIAFF KTQFTQPGDF TYWFVGNYDE
GTLIPLIERY LGGGTASVEK MSWVDRGIRP PTGMVSEAIY KGSEPKSSVV MTFSEQKKYK
RKDSYYIKAF SEVLDIKLIE ILREEKGGVY GVGASGQGHL RPYEHYSTQI QFPCAPENVD
TLVRAALDVV RDIQQNGVSE EDLNKIKETQ RRDMELNWKE NGFWLGAMKS YVKNDLDLSK
INELNERIEE LSAKDIQTAA KKYVDTEEYI RIVLYPETTE
//
