ID A0A1F4PLC0_9BACT Unreviewed; 881 AA.
AC A0A1F4PLC0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3F66_00050 {ECO:0000313|EMBL:OGB84643.1};
OS candidate division TM6 bacterium RIFCSPHIGHO2_12_FULL_32_22.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1802375 {ECO:0000313|EMBL:OGB84643.1, ECO:0000313|Proteomes:UP000178609};
RN [1] {ECO:0000313|EMBL:OGB84643.1, ECO:0000313|Proteomes:UP000178609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB84643.1}.
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DR EMBL; METJ01000009; OGB84643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4PLC0; -.
DR Proteomes; UP000178609; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:InterPro.
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; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
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;
FT DOMAIN 30..166
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 183..361
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 500..629
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 642..814
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 881 AA; 101844 MW; A765FD00D357C248 CRC64;
MKKLIILLLT VTAVNGIPEF KEYTLKNGLK VVVQPSPNTP DVSIKLYYHV GSKDEKESEK
GLAHLLEHMI FKGTQKLSET DIDLAASKLS GWCNANTYYD RTCYEFNLPK RHWQEALPIL
ADCMTNCRFQ DDHLNSEFKA VIQELKMGRD NPGHPMFFRI MNNIFPDHPY HFPVIGYKQD
IWNVTGKDLH KFYKKHYLPN NAILVVVGDV DSEEVSTLSE KLFGHIKANF DYKKKKTFLN
SDITSTSTKI YRDIQTPTVW LSFLIPGLNA KQVHLIDCIK TALAGDQFAR LNKILVEEKQ
LVHAIQIYEV VLFEYGLFII AFDPKNIDNI NEIQSIIFSE LKKLETENLT SFEIKKIVNQ
LKSFNYELLQ DNKTKAALIG EYYLAAKDYI YPFQCFELKK ENLNQEIKKF ISTYLREAIA
HQVIILPIPE SEKENWKKIQ EEGDAEDLEI LNQRIRESEV EKPKYSNNIY PKELEKIETK
RPEEFILSNG IKVFFVEDKI SPKVDLLLVL KASPEYEPAD KPEIYALLTD SMFRGTKNKN
YNDIVNLLTK NAINFVVDKN KFSISCLTKK LTKACKLLNE ILTEPEFQEE DINKIKDQMK
NNIKNFWDTP QSISEYLLNN AIYKDHIKKA TCPTSEQIDN YNKEELLNLY KQFITPDKAT
IFVSGDIEVD KLKEILESIA KWFGNKIEES NCDDISETKA DTVHHKIDRD QTHLTIATKS
ISYKDENFHN LLIASHILSS GMSSKLFQIR QQTGLFYTVS GSFLKDVTET AGMFIIKTIV
SKDNVDKSKE IFLNLINNFA DTITEADLKR AQDAILDSLA KKYVTRVSTI NNIYNLYINN
LGWDFYRDLT DKVKNTTLAD LKKSVKEFFK DKEFVTITVG R
//
