ID A0A0D5YPF6_9FLAO Unreviewed; 362 AA.
AC A0A0D5YPF6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Metallopeptidase, family M42 {ECO:0000313|EMBL:AKA33716.1};
GN ORFNames=VC82_22 {ECO:0000313|EMBL:AKA33716.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA33716.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA33716.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA33716.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-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}.
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DR EMBL; CP011071; AKA33716.1; -; Genomic_DNA.
DR RefSeq; WP_045800590.1; NZ_CP011071.1.
DR AlphaFoldDB; A0A0D5YPF6; -.
DR STRING; 516051.VC82_22; -.
DR KEGG; mlt:VC82_22; -.
DR PATRIC; fig|516051.4.peg.22; -.
DR HOGENOM; CLU_047249_1_0_10; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000032726; Chromosome.
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 CDD; cd05656; M42_Frv; 1.
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:SF20; AMINOPEPTIDASE YSDC-RELATED; 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:UP000032726}.
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 362 AA; 40709 MW; 06037A11180EEBF4 CRC64;
MAASKILTKK SLEFFEKYLN NASPTGYEWE GQKIWMDYLK PYVDDFITDT YGTAVAVINP
DAKYKVVIEG HSDEISWYVN YITDNGLLYV IRNGGSDHQI APSKWVNIHT KNGVVKGVFG
WPAIHTRDKS KEQPPKIENI FIDIGAKDKE EVEKMGVHVG CVITYPDTFQ ILNNDKFVCR
AIDNRAGGFM VAEVARLLHE NKKKLPFGLY ITNSVQEEIG LRGAQMITET IKPNVAIVTD
VTHDTTTPMI DKKKEGETSI GKGPVISYAP AVQQKLRERI IETAEAKKIP FQRQASSRST
GTDTDAFAYS NGGVASALIS LPLRYMHTTV EMVHRDDVEN VIRLIYETLL TIKEGETFSY
FE
//
