ID A0A3R8M2G3_9CAUL Unreviewed; 894 AA.
AC A0A3R8M2G3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=EIK80_21185 {ECO:0000313|EMBL:RRN62604.1};
OS Caulobacter sp. 602-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN62604.1, ECO:0000313|Proteomes:UP000268773};
RN [1] {ECO:0000313|EMBL:RRN62604.1, ECO:0000313|Proteomes:UP000268773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=602-1 {ECO:0000313|EMBL:RRN62604.1,
RC ECO:0000313|Proteomes:UP000268773};
RA Gao J., Sun J.;
RT "The genome of Caulobacter sp 602-1.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:RRN62604.1}.
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DR EMBL; RRYI01000008; RRN62604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8M2G3; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000268773; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..894
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018787325"
FT DOMAIN 61..238
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 272..489
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 565..870
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 431
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 894 AA; 95677 MW; 05D6B808F67ADB1A CRC64;
MRRLMSSAAV AVILFAAGGV SAAASGHLQV KPKPAAVAAQ AGSKGATFAT VTTQLPRAVR
PTHYDLSFTP DADKMAFTAS VKIAIEVVEP TATVTLQAAD LAFSKAEIAG VGAAKVKVDD
EAQTASFTFA KPLPKGKYVL ALDYTGKIYT QAAGLFALDY ETETGKKRAI YTQFENSDAR
RFIPSWDEPF YKATYSVEAT IPTGQMALGN MPIASSKDLG NGKTLVKFAT SPKMSTYLLF
FGLGEFDRAS VKAAGADVGV VTKKGDTPKA QFALKAAADI LPWYNDYFGT PYPLPVLDNI
AAPGRSQFFS AMENWGAIFY FEYALLLDPK ISTESDKQTV FTTVAHEMAH QWFGDLVTMA
WWDDLWLNEG FASWMEGRAT EHFHPEWNAN LNAVGGREYA MGLDALSTTH PVVQHVTTVE
QASQAFDGIT YQKGEAVIRM LESYVGHDAW RDGVRAYMKK HAHGNTVSDD LWSSVEGAAK
KPITAIAHDF TLQPGVPLIT VDAATCAAGK TTLTLTQGEF SKDMPGKKPL LWRVPVTVRA
IGGGEAKTLV TGGKGSVTVD GCGPVVVNAG QNGYFRTQYG AERFGGIVQS FAKLPAIDQL
GVMSDAWSMG LAGYQPATDF LDLAKATPAD ADPQVFSKIA GVYSSIDNYY EGMPTERAAF
RKLAVAKLRP LLARVGWTAR SGEPDSTAIL RGELIGTLGG LGDPEVVAEA TRRFNADKTD
PSAIPGPLRK TILSVVARHA DAATWDAIHA QALAEKTPLI RAQLFSLLAS AEDEALARKA
LELALTPEPG ETMSSTMISR VASAHPDMTF DWAVANKDKV NEKVDSTSRT RFIPGLGAGS
SNPAMAEKIK AWAAANLAEG SRKEADKAAA SVLNRAKIRE QRLPAITAWV GKNG
//
