ID   A0A1J5FC77_9BACT        Unreviewed;       763 AA.
AC   A0A1J5FC77;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Neutral metalloproteinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUK12_01020 {ECO:0000313|EMBL:OIP57901.1};
OS   Candidatus Levybacteria bacterium CG2_30_37_29.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1805237 {ECO:0000313|EMBL:OIP57901.1, ECO:0000313|Proteomes:UP000182355};
RN   [1] {ECO:0000313|EMBL:OIP57901.1, ECO:0000313|Proteomes:UP000182355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_37_29 {ECO:0000313|EMBL:OIP57901.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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:OIP57901.1}.
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DR   EMBL; MNYS01000003; OIP57901.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5FC77; -.
DR   STRING; 1805237.AUK12_01020; -.
DR   Proteomes; UP000182355; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          133..169
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          303..378
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          387..531
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          555..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..589
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   763 AA;  82276 MW;  DBD301AE698E4390 CRC64;
     MFENYYQKIR SILAVYRREI IIFACILFVV FLIIFVLFLI KKLKPQVVPV TLSSYSRIIL
     DKNRSYFSIN TENGYLYKTK REGQEAIDEF LKSNGKVNGQ DLLPNNFYKN SKIIRVAKDS
     ELNPKYSTSS NSKEHYFLSQ KINGIPIYGA SLIIHLQNKN EIYSISGNIA TNDSITKEKI
     SEKEAVGIAT NQAAKDSSYA TDLVVKDSSK SILNLKLLGL SEDVVNHLTL AVQFDSAKNF
     FSKRYYVDLS NRKMLYSEDL ITQVMTRKVY DCNGTSNPPC SLRRSEGEPP MGDLDGDSLY
     DLMGEVYNYY FNTFGRDALD GAGAPLQGIV NIYSVNGTPC SVFSNAYNTG GAGGGIMAYC
     KGTATRDIAA HEFTHGVVST TAGLAPGYQY GALNESLADS FANAIDNNWT MGEGSALGII
     RNMSNPPSSR NDPDKLFSST YDCVGEEVHK NAGVPNKAFY LMTDGGSFNG CSMSGIGTVK
     SHEILYKALT QYLSSTANFF DLYSGVNQAC NDIHGASSTT CEEAKKAYQA TEMDQQTPGS
     SRGAKCTGRV EQTATCAGGS FGPTNTPTPS PTPGGPANTP TPSPTPGGST ATPTPIVASS
     GLWKLKATPI CSGNVSNISY DYEIPSGERA VIETINSAGN PLGIEDMSSW VGGPPYIVGN
     GTYIAKGNRL SPVDSGLKNN YGYTSEYHYG TPGHVISLIL TLNVKTLDCT NPPLPTSTPT
     PGGPINTSIP TPTPQKTYTC VPDPTCVSSG KVIQMCPLKC TEN
//