ID I6B166_9BACT Unreviewed; 957 AA.
AC I6B166;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:EIQ01008.1};
GN ORFNames=OpiT1DRAFT_05569 {ECO:0000313|EMBL:EIQ01008.1};
OS Opitutaceae bacterium TAV1.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278956 {ECO:0000313|EMBL:EIQ01008.1, ECO:0000313|Proteomes:UP000004921};
RN [1] {ECO:0000313|EMBL:EIQ01008.1, ECO:0000313|Proteomes:UP000004921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV1 {ECO:0000313|EMBL:EIQ01008.1,
RC ECO:0000313|Proteomes:UP000004921};
RX PubMed=22535930; DOI=10.1128/JB.00264-12;
RA Isanapong J., Goodwin L., Bruce D., Chen A., Detter C., Han J., Han C.S.,
RA Held B., Huntemann M., Ivanova N., Land M.L., Mavromatis K., Nolan M.,
RA Pati A., Pennacchio L., Pitluck S., Szeto E., Tapia R., Woyke T.,
RA Rodrigues J.L.;
RT "High-Quality Draft Genome Sequence of the Opitutaceae Bacterium Strain
RT TAV1, a Symbiont of the Wood-Feeding Termite Reticulitermes flavipes.";
RL J. Bacteriol. 194:2744-2745(2012).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; JH660698; EIQ01008.1; -; Genomic_DNA.
DR AlphaFoldDB; I6B166; -.
DR HOGENOM; CLU_008156_0_0_0; -.
DR Proteomes; UP000004921; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..957
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003702303"
FT DOMAIN 48..172
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 208..256
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 703..882
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 253..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 104044 MW; 98A323E5E83D34BD CRC64;
MRLLTAFLLA GLLVSSAFAA DAAAPAVTAL RPDPELREGT LDNGLRYIVR RNSEPQHRAS
LRLVVLAGSF HETDAQRGLA HFLEHMAFNG STHYPPRTLI KFFQRMGMGF GGDTNAWTSF
DHTAYLLELP DTKPETLAEG LRVFGDYAGG LLLDPSEIDR ERGVILSEKR TRDSAEYRAS
IASYEFLFAG TLLPRRLPIG EESVIKNATR DDFLDLYNTW YRPERMAVIA VGDFDPDAVV
AEIKNNKNLA SVADRAPARP EPDMGKLAAA DRPGDDAASS AGILASAHYE SDAGATTVSI
NAIRPWNREP DSVQKRLREL PRDLASAMLN RHLEILAKKE NAPFSQASVS IGEYFRFIHS
ASLRLTTTPD HWSDALATGE QELRRALQFG FRESELREAR ANYKNALEQA VKTDPTRDSP
DRASELIDSV VDEIVPTTPA DDLALLGPAL DAITPEDCHE ALRADFSTPA GLQVFVAGNT
RLAEAADDAS AAIVAAWKKS ADSPVTPSAD TAADAFAYTD FGPAGKITER RHIDDLDVTL
VTFANGLRLN LKKTDFKTGE IQVRARVGTG RLRLPGNQPG LDFYAGLTFT AGGLGKHSTD
DLRSLLAGRN VGVGFNVADD AFVFSGVTTP ADLLLELQLL AAHITDPGYR PEAARLAEKN
LEQFYTRLAH SASGPLQTIV PRLLASGDPR FGLPTRAEAS DRTLGEVKAW LAPHLASGAI
ELAVVGDIDI DATLQAVAAT LGALPDRAPR PARDALADVL RVDVPAKSVE ETFTVPSTIP
KGIVALWWPT RDALDATPAR RLNLLADIFT DRLREVVREK IGGAYSPYAA SAPSDVFPGY
GFILTNITVD PGHAVEIAAA VTRIAQELHD DGVTDDEITR ARLPVLTALR ESARTNEYWL
GIVLAAAQEQ PQRLDWARTR YSDYESITKA DIDALAKTYL APDRAFRFTV LPVDEKK
//