ID A0A1G3QS04_9SPIR Unreviewed; 525 AA.
AC A0A1G3QS04;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=A2V99_00250 {ECO:0000313|EMBL:OHD69487.1};
OS Spirochaetes bacterium RBG_16_67_19.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802196 {ECO:0000313|EMBL:OHD69487.1, ECO:0000313|Proteomes:UP000177018};
RN [1] {ECO:0000313|EMBL:OHD69487.1, ECO:0000313|Proteomes:UP000177018}
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:OHD69487.1}.
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DR EMBL; MIBK01000240; OHD69487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3QS04; -.
DR STRING; 1802196.A2V99_00250; -.
DR Proteomes; UP000177018; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 119..184
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 340..501
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT NON_TER 525
FT /evidence="ECO:0000313|EMBL:OHD69487.1"
SQ SEQUENCE 525 AA; 58248 MW; 4C8BD51A91E1EA1E CRC64;
MSQPNTSASQ VWDLRSFFPD FNGPEMLSYK EGLRAEVSSL QERAAGAGPL TAATAETWEG
IVLSLEEVEA RLGHITAYVE CLGAADAGNE AYAREEALLA LMGAETEKAE VDLLQAFKAA
GDELFAAFSG REKLRDAAHR LRRLRRRARR TMPREQERLA ADLAVDGLHA WGRMYNTLSG
KLDFEMKWPD GRVQRVPMAQ WRALMSSADR RVGRAAFEGG NREWARVGDA CAAALNAIAG
NRLTLNRYRG HGHYLEPALH QSQVEPETLE AMYAAIHANL ELPRRIFRAK ASAFGRTGIW
WFEREAPLAL GGSGEMDWEA GSRMVGRAFG QVYPGLADYF RLALEKRWIE SEKRPGKRPG
AFCTGSELTG EQRIYMTFAG ALRDASTLAH EAGHAWHASL LRDLRPMARG YPMTLAETAS
VFAEQILTQG LAADPGLPDG QKLLMLDGEL GDAAIMLLDI TVRYEFERSF HDERAAGEVG
VTRLGELMTA AQRRLWGDAL LPDGTDPWFW ASKLHFYIKQ AALLH
//
