ID A0A095Y6T5_9BACT Unreviewed; 969 AA.
AC A0A095Y6T5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KGF17983.1};
GN ORFNames=HMPREF1640_05515 {ECO:0000313|EMBL:KGF17983.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF17983.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF17983.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF17983.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KGF17983.1}.
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DR EMBL; JRNC01000031; KGF17983.1; -; Genomic_DNA.
DR RefSeq; WP_036892880.1; NZ_JRNC01000031.1.
DR AlphaFoldDB; A0A095Y6T5; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000029597; 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; 4.
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; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029597};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..969
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001913353"
FT DOMAIN 49..99
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 251..424
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 713..877
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 969 AA; 110268 MW; 7D2A5FF3449295DE CRC64;
MKFKLITASL ATFLALTISA KDYHYKSVAG DPMQTRIYTL DNGLKVYLSV NKEKPRLQTY
IAVRTGSRND PAETTGLAHY LEHLMFKGTK LYGTSDALAE APLLDEIEQR YEDYRRLKDP
VSRKNAYHEI DSVSQIAAKY NIPNEYDKIM RSIGAEGTNA YTSNDVTCYV NDIPANEIES
WAKVESDRFR NMVIRGFHTE LEAVYEEFNI GLANDSRKMW EAMFKKLFPT HPYGTQSTIG
TQEHLKNPSI TNIKNYFNRY YVPNNIAICM AGDIDPDKVM AIIDKYFGDW QRSSTLSRPE
YAPVADLVAP TDTTVIGQEA EHLMIGWKTP NAASYDTDTL RVIADILSNG KAGLFDVDLN
QPMRVQSASA FSEGLHDYGM FVLYAVPTQG QSLEEAKGLV LAEMEKLRKG QFDEKLLRAV
VNNLKLDYYK SLQSNSDRAD KFVKAFINEC KWEDEVRALD RISNMTKRQI VDYANRHLRD
NYVVAYKKKG VDNSVKKIDK PAITPIPTNN DMQSDFLKDI VNAKVAPIEP RFVDFSKDLS
KRDVDAKTVL LYKKNDSDGL FNLEFDIPVG RENDSRLHMA SALLDYAGTA KMSANDIKKA
FYDLACNFNV SVRPNHTRLS LSGLNENMPA ALKLFTNLLE HATISKADYD KVVGLVLKSR
QDSKQSQGGT YMALISYGVY GKTSPYLNSM TEEQLKASDG NELLLALRNA RHLNPMTIMY
YGPTDEKTLL SLVKKDYPRR HVKATQPLNT VRYTAQPTPK NEVLLAHYDA KNIYMVQYNN
ANRVWNMDNA PLVSMFNEYF SGGMNAIVFQ ELREARGLAY SASARYNAPY RLGDKEYFNT
FIITQSDKMM DCIGEFNNLL NQIPQNQAGF ELAKQSLLKS LATNRHTRFN TLNYYMTMRE
LGLNYDIDQK IYDKIPSITL DDIVNFAKER IANKPYKYLI VGDEKNLDTK SLEKIAPIRR
VSEKEIFGF
//