ID R7BPM2_9ACTN Unreviewed; 418 AA.
AC R7BPM2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Protease {ECO:0000313|EMBL:CDD67462.1};
GN ORFNames=BN629_01117 {ECO:0000313|EMBL:CDD67462.1};
OS Eggerthella sp. CAG:368.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=1262877 {ECO:0000313|EMBL:CDD67462.1, ECO:0000313|Proteomes:UP000018088};
RN [1] {ECO:0000313|EMBL:CDD67462.1, ECO:0000313|Proteomes:UP000018088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:368 {ECO:0000313|Proteomes:UP000018088};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD67462.1}.
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DR EMBL; CBHM010000053; CDD67462.1; -; Genomic_DNA.
DR AlphaFoldDB; R7BPM2; -.
DR STRING; 1262877.BN629_01117; -.
DR Proteomes; UP000018088; 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; 2.
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; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CDD67462.1};
KW Protease {ECO:0000313|EMBL:CDD67462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018088}.
FT DOMAIN 13..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 174..337
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 418 AA; 46778 MW; 05313105B8B7B8D7 CRC64;
MSFQKTILDN GIVVITEYMP SVRSISLGLW FNVGSCDELP NQRGLAHFME HMMFKGTPTR
TPFDISMHFD RLGAEFNAFT SKEYTCYYAR FVDDKLESAL EVLADMVINS SFSTEAISTE
REVVLEEIAR SEDTPDDYVF ELFNQSMITD HALGLPVLGD KRLVSSYEHV DCVSFHDQHY
GSGNLCIAAA GNIDHDALVK LTQAYFSSMN TLEKEQRNQD RVAYQSGCFS VTRDIEQAHI
IYGVPGLALG DDRRFASGVL TSILGGSMSA RLFQEVREKR GLAYSIYAMQ GIYQRAGQWC
VYAGTRPDNV KEVIRLIDKE LTSLADGSLD QDELQRNVDL ICGQAVLGYE TTSSHMMRLG
KRGILGSQHL SIDETIERFK QVTVEEVVSI AETLFSNKPT IAVVSPLEEK ELQALISE
//