ID A0A1H5U010_9GAMM Unreviewed; 377 AA.
AC A0A1H5U010;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Hydrolase, peptidase M42 family {ECO:0000313|EMBL:SEF68330.1};
GN ORFNames=SAMN05444390_101222 {ECO:0000313|EMBL:SEF68330.1};
OS Marinobacterium lutimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=568106 {ECO:0000313|EMBL:SEF68330.1, ECO:0000313|Proteomes:UP000236745};
RN [1] {ECO:0000313|EMBL:SEF68330.1, ECO:0000313|Proteomes:UP000236745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22012 {ECO:0000313|EMBL:SEF68330.1,
RC ECO:0000313|Proteomes:UP000236745};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNVQ01000001; SEF68330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5U010; -.
DR OrthoDB; 361940at2; -.
DR Proteomes; UP000236745; 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 CDD; cd05657; M42_glucanase_like; 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 InterPro; IPR017537; Peptidase_M42_hydrolase.
DR NCBIfam; TIGR03106; trio_M42_hydro; 1.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF7; AMINOPEPTIDASE YHFE-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, ECO:0000313|EMBL:SEF68330.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000236745}.
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 377 AA; 41726 MW; 511871EF5AA158A0 CRC64;
MTKLQIDQEY LKEQLKNLLL TPSPSGMTDD AVRYVCGELE KLDIRYELTR RGAIRAIIPG
KNDSPRRAIA AHLDTLGAMV KGLKREGRLR VVPIGHWNAR FAEGARVKVH CDNGQVYTGT
ILPLKASGHT YNKGVDEQPS DWSNLEIRID EPVNQIDQLW DMGVRVGDFV SVDSKPEFCP
SGHINGRHLD DKAGVASMLA AAKAMMDADV KPELDCHLLF TISEEVGVGA SHVLHGDIAE
MVSIDNGTIA PEQNTCEYGV TIAMQDSSGP FDRPLTQHLI NICKREEVEF SRDVFLYYRS
DAASALEAGN DIRTALICFA LDASHGWERT HIGSLESVAS LLVGYMRSKP LFAEHENVIG
DESEYPLIAA DRERLKM
//
