ID A0A0N8GMV4_9CHLR Unreviewed; 359 AA.
AC A0A0N8GMV4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=M42 family peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC812_06695 {ECO:0000313|EMBL:KPL76346.1};
OS Bellilinea caldifistulae.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Bellilinea.
OX NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL76346.1, ECO:0000313|Proteomes:UP000050514};
RN [1] {ECO:0000313|EMBL:KPL76346.1, ECO:0000313|Proteomes:UP000050514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL76346.1,
RC ECO:0000313|Proteomes:UP000050514};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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:KPL76346.1}.
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DR EMBL; LGHJ01000012; KPL76346.1; -; Genomic_DNA.
DR RefSeq; WP_061919374.1; NZ_LGHJ01000012.1.
DR AlphaFoldDB; A0A0N8GMV4; -.
DR STRING; 360411.AC812_06695; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000050514; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF5; ENDOGLUCANASE; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000050514}.
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 359 AA; 39081 MW; B6484BD27BD04E25 CRC64;
MSEYSPFSQP VSKSQLDLLE RLSNAVAVSG DEREVRAIVL EEIQPFADEV RVDALGNVLA
VRHAQEENPL RVMLAAHMDE VGFILVEEEE GGWYRFEVVG GIDPRVLVGK PVLVGKEHLP
GVIGTRPIHL TTPDERKNAL TVEQLRIDLG NENGKKVKTG ERAGFATRFR QAGPSLVGKA
LDDRLGVAAL IELIKNPPPN VELQAAFTVQ EEIGLRGAGV AAYAFNPDVA IAVDATPAND
LPAWDGEENT RYNTRLGGGP AIYVADAATL SDPRLIRHLI RTAEEMGIPY QIRQPGGGGT
DAGAIHKQRE GIPVVSVSVP VRYAHTPALQ ARLLDWENTL SLLYHGLERL SPQLFSEDR
//
