ID A0A1G2NCE3_9BACT Unreviewed; 589 AA.
AC A0A1G2NCE3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=A2928_00525 {ECO:0000313|EMBL:OHA33022.1};
OS Candidatus Taylorbacteria bacterium RIFCSPLOWO2_01_FULL_45_15b.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802319 {ECO:0000313|EMBL:OHA33022.1, ECO:0000313|Proteomes:UP000176221};
RN [1] {ECO:0000313|EMBL:OHA33022.1, ECO:0000313|Proteomes:UP000176221}
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:OHA33022.1}.
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DR EMBL; MHRX01000036; OHA33022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2NCE3; -.
DR STRING; 1802319.A2928_00525; -.
DR Proteomes; UP000176221; 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 CDD; cd09610; M3B_PepF; 1.
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; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 231..575
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 589 AA; 67469 MW; B615E3BC2E1DA69E CRC64;
MKRNRHKQKT EWDLRALYAS PNDPKIESDV KRLEARAKEF NKKYNTSRAW LGSPNELNKV
LQEYEDIVCS VGTFKPLLYF SYLRALGARK SEYDARIALL TPRAQHISNL LLFFELELAK
LDGAVRQKFL KAGILVGRRY LLKRIFDSAK HNLTLSEEKI MNLKSQTSYD MWVEVVERIL
SSKTVLYKGK KIPLPQAQNL IPQLSLKDRR LLHVLLNDVY KEIAPIAEAE INAIVINKKT
NDELRAFEKP YSQTVLSYQN DPKTVEVLVK TVTDNFSISK DFYAIKAKLL GVKKLTYADR
TASIGSIKRS FKFDEATKIV RDSFAKAHPE FAEVLDDMLK MGNIDAFPKA GKQGGAFCSS
GYKTPIYVLL NHTNSFNDVR TYAHEMGHAI HAHYSRGQRP LYSGHSYATA EIASTLFENF
VFDAVFDSLN ESEKKIALHD KLNSSVSTVF RQVACFNFEN QLHTAIRKNG YLSKEEIASL
LKKNLEQYMG PVMKLIPDDG YFFVTWSHIR RFFYVYSYAF GELVSNAMYA EYKGDPKFIN
KIIEFLKAGE SDTPENILRG IGIDVTLPNF FLQGLNEIKS EMLDFKQIV
//
