ID   L8JLA4_9BACT            Unreviewed;       949 AA.
AC   L8JLA4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Putative peptidase {ECO:0000313|EMBL:ELR68244.1};
GN   ORFNames=C900_00598 {ECO:0000313|EMBL:ELR68244.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR68244.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR68244.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR68244.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-2012) 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:ELR68244.1}.
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DR   EMBL; AMZN01000128; ELR68244.1; -; Genomic_DNA.
DR   RefSeq; WP_009583499.1; NZ_AMZN01000128.1.
DR   AlphaFoldDB; L8JLA4; -.
DR   STRING; 1237149.C900_00598; -.
DR   PATRIC; fig|1237149.3.peg.5678; -.
DR   eggNOG; COG0612; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000011135; 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:SF21; PROCESSING PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000011135};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..949
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003994041"
FT   DOMAIN          48..137
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          205..383
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          535..649
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          677..854
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          479..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  105873 MW;  BC5926D8C0689D93 CRC64;
     MRNCYLSMLM IILLLVQSCT QVAEKSVEGA ENLSIEYDKI TLPNGLDVIL HQDKSDPIVA
     VAILIHAGSN REKPGRTGFA HFFEHMLFQR SENVPEGAFF KNINEWGGTF NGGTWTDGTV
     YYEVVPKDAL EKVLWMESDR MGFFINSVTK ASLEGEKPVV KNEKRQRYDN VAYGNTSAVI
     NKALYPPNHP YNWLTIGELE DLQNATLDDV KEFYDQYYGP NNATLVLTGD FDKEEAKKMI
     EKYFGEIPSR GVDKPLDPQP VTLDSTIALY HEDNFASLPE IRMVWPTVEQ YHQDQWALDV
     LGNILSDGKR APLYKVIVED RELAPEVSAN NRSSELAGTF TIRIRANEGV DLDSVKTEVF
     NALVKFENEG VNIKDLDRIK AGLETNFYNG ISSVLGKAFQ LATYNEYAGS PDFVKTDIGN
     IKAVTQEDVM KVYKKYIKDK HYVQTSFVPK GKLDLAVTGG KAAELKEEAI VPGTETAIVD
     QEPSDDYPRT ESSFDRTQEP PFGEAPLLNP PAIWTSELSN GMGVYGIEYN ELPLVNFSIR
     IAGGHMAEDL SKAGLTNILT DLLMEGTRSK TPEELEDAIG QLGANINVYT SDESITISAN
     CLSRNYEATL NLVEEILLDP RWDAKEFDRI KKAAINKIQQ RDVNPNSLAA IVMDKKLYGK
     DNILGAPISG TIESVESITM DDLKAYYDKY FSPSIANFHI AGNVPKDDVK ASIASIGNKW
     TAKEVTLPEM EIPASAEQPQ VYFVDVPNAK QSVIQIGRVT VDGNNKDFYP LTVANYRLGS
     GSGGRLFQVL REDKGYTYGA YSYVGRKKIK GPFIAASSVK SNVTLEALET FKEVIGNYAD
     TYTEEDLEKT KSALIKTNTR NFETLYSLVG ILQTISTYDL PLNYIDHQQE ILKNMTTEDV
     KALVNKYMDL KNMVYVIVGD KATQFERLKV DGMGNPVLVD KNGNEITVM
//