ID F3PSG3_9BACE Unreviewed; 930 AA.
AC F3PSG3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:EGF57617.1};
GN ORFNames=HMPREF9446_01697 {ECO:0000313|EMBL:EGF57617.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF57617.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF57617.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF57617.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGF57617.1}.
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DR EMBL; AFBN01000028; EGF57617.1; -; Genomic_DNA.
DR AlphaFoldDB; F3PSG3; -.
DR STRING; 763034.HMPREF9446_01697; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_008156_0_0_10; -.
DR Proteomes; UP000003416; 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: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.
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:UP000003416};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 43..168
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..385
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 682..860
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 930 AA; 105549 MW; 616B699CE603DB2D CRC64;
MVALIVCCNF QQVSAQQMPP IPVDKNVRIG KLDNGLTYYI RKNNLPANRA DFYIAQKVGS
IQEEANQRGL AHFLEHMCFN GTTHFPGDAL KQYLERIGVK FGENLNAYTS IDETVYNISN
VPVTTPGAID SCLLILHDWS NDLTLDPKEI DKERGVINEE WRTRMSAIQR FQEKMLPIMF
EGTKYAHCFP IGTMDVVMNF KPQTLRDYYE KWYRPDLQGI VVVGDVDVDA IEAQIKKIFS
DIPAQPNGAK REYYPVNDNK DPIVIVYQDK EQPNIQAIIF NKHEAIPDDQ KGNMGYLIQN
YAANLITNML NARLNELAQT ANPPYIYAGA YDANFFVAKT KGAFTGVVVC KEDAIENGIE
TLLRETERAR QFGFTETEYN RARAEYLRHL ESAYNERDKR KNEEYVNEYV RHFLDNEPIP
GIENEYTIIN QIAPAIPVTA LNQMMQELVT DSNQVVAILG PQKEGLKMPS ENAIKQILKD
IKAEKLTAYV DKVSDEPLMK AAPKGGKIVS ETTDDAFGTT MMTLSNGVKV IIKKTDFKAD
EIRMKGVSLG GSSLFPDSEI ININGLDAVG VGGLGNFSAV DLEKVLAGKK ASVSYGIGDK
TEAVNGSCSP KDFETMMQLT YLTFTAPRRD NDAFASYKNR NKAALQNMEM NPQVAFSDSV
QAGIYMKHPR KVRIKADMID KMDYDKILSM YNDRFKDASD FTFIFVGNVD VEQMKPLIEE
YLGALPAINR KETFKDNKID MRQGVYKNEF IRKQETAKAS NFVLLNGDCK YDLRNNILLN
MTCQILDLVY TAKVREDEGG TYGVYVGGQL IKYPEEKAIL QVIFETAPEK REKLMKIIFA
ELENITKAGP SETDLNKVKE FMLKKHTEDM KENRYWLNSI DEYLFTGMNP IKDYDRIVNS
VTVKDIQKFA DELFKQKNEI EVSMISPEEK
//