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Database: UniProt
Entry: A0A136KHP6_9BACT
LinkDB: A0A136KHP6_9BACT
Original site: A0A136KHP6_9BACT 
ID   A0A136KHP6_9BACT        Unreviewed;       926 AA.
AC   A0A136KHP6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Bacillolysin {ECO:0000313|EMBL:KXK08823.1};
DE            EC=3.4.24.28 {ECO:0000313|EMBL:KXK08823.1};
GN   Name=npr {ECO:0000313|EMBL:KXK08823.1};
GN   ORFNames=UZ21_OP11001000378 {ECO:0000313|EMBL:KXK08823.1};
OS   Microgenomates bacterium OLB22.
OC   Bacteria; Candidatus Microgenomates.
OX   NCBI_TaxID=1617428 {ECO:0000313|EMBL:KXK08823.1, ECO:0000313|Proteomes:UP000070562};
RN   [1] {ECO:0000313|EMBL:KXK08823.1, ECO:0000313|Proteomes:UP000070562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB22 {ECO:0000313|EMBL:KXK08823.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KXK08823.1}.
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DR   EMBL; LLEV01000006; KXK08823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KHP6; -.
DR   STRING; 1617428.UZ21_OP11001000378; -.
DR   Proteomes; UP000070562; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; 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; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR036439; Dockerin_dom_sf.
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; 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, ECO:0000313|EMBL:KXK08823.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          311..413
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          417..564
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          590..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          716..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        483
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   926 AA;  99079 MW;  DFD13413A7702244 CRC64;
     MKSAQFEHNP FIQFILAGLG LYAVVMLTML SVDLLSPRQQ VKTKATGQPQ FDVSQVEQDQ
     AIAGVLDGTI TVDVSSNKGL ITIPSDSSTD VAAAVKALEV LENTPLSLIP SDDMVQGIST
     SDEITILPEG FSRTAKLVRT LDEAKVFTQA AAAPVKHYYF QQQIKVEGKL VPVFGTDARV
     SMMQQDEEET VIGVGATVLG INPEPDALVM QTGSTDTQLL VDKAQAQAKV FLDNPALNVS
     LCVGSALEDE IVNKSILGIS SDTTNYLTKR VPLCVDEQQD IKVLNVFIDP QTQEAIFIEP
     LIYDALQRRV SDCSTGSCQV KRTEGSGPSN SAEADKAYDL LKKVYDYFKT KHNRDSFDGR
     GAPLVAEVNY SGAIASAGGA RCPNAVWLGA KMAACRGLVL DDVWAHEITH GVTFTTSNLL
     YQNQSGALNE SFSDIFGWAV DPDDFAMGNI RRLDDPTRSQ RPQPDKLFSP LYHTKSTDQG
     GVHINSGILN KAFYLMVAGG NFNDCTIQKA DPERVLEAIY KALTVYLNRT SNFKSAYTAI
     NRACADIHGA SSPTCATIEA SMQATQMDQM GSGQTCPECN STRGKVATCA GKGPQGGGDS
     QPPQNPQPSG STRVPANPPR STATPRPTAR IGGSPNTGNR YPTTSQRAPT GSAESPVGGN
     VKSIDPVTEC PVTAPTSVER AYSAVRVTCT DGRSSLLQKQ TCTPLGGYKA DATTFCAGSS
     PPAPRDGGEN TPAPVPGNPQ ETGDTVAVVF QVQLQGVTDK IPPQHAIIPM RVGLSSRALD
     RPLYVDTEAK ARLDGKTVLW EGKAIFKADP RLSYQILLKG PVHIQRKFCH EVVQEREPGA
     YLCAGSSIPV SQGTIHLNAS TVPLFACDVP EQNGICNSLD LSVIKDGIGS IQPAIIIRCD
     MNLDGVCNAQ DYVIALQAFL IRLDEE
//
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