ID A0A0L6CGS5_9MICO Unreviewed; 860 AA.
AC A0A0L6CGS5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=VV01_05435 {ECO:0000313|EMBL:KNX36718.1};
OS Luteipulveratus halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=1631356 {ECO:0000313|EMBL:KNX36718.1, ECO:0000313|Proteomes:UP000037397};
RN [1] {ECO:0000313|Proteomes:UP000037397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C296001 {ECO:0000313|Proteomes:UP000037397};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:KNX36718.1}.
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DR EMBL; LAIR01000002; KNX36718.1; -; Genomic_DNA.
DR RefSeq; WP_050668998.1; NZ_LAIR01000002.1.
DR AlphaFoldDB; A0A0L6CGS5; -.
DR STRING; 1631356.VV01_05435; -.
DR PATRIC; fig|1631356.3.peg.1029; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000037397; 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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09602; M1_APN; 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; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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:0000313|EMBL:KNX36718.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037397};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..199
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 242..455
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 538..848
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 719..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 94582 MW; D6778A1889405AA2 CRC64;
MPGKNLTREE ARTRADLLAV ESYDVTLDLT TGPETFSTRS EVTFGARTAG AESFIDFIGD
SVQSITLNGE SLDPATHFAD NRIALPGLQE SNELVIESTG RYMNTGEGLH RMVDPTDQEV
YLYTQFEVAD CRRMFAVFEQ PDLKATFRFT VTAPQRWEVI SNQPAPEPVA AQGSYTNPKG
EQEPTATWAF EPTERMSCYI TALVAGPYDV VRDEVQTRNG TVPLGVYCRK SLRPYLDADN
IFDCTKKGFA FFEEEFDQPY PFSKYDQLFV PEYNAGAMEN AGCVTFTEVY VFRAKVSDAI
VERRALTILH ELAHMWFGDL VTMQWWDDLW LNESFAEWAS TTCQAEATQW ESAWTTFGTA
EKAWAYNQDQ LSSTHPIAAD ITDLEAVEVN FDGITYAKGA SVLKQLVAYV GREPFVAGLR
TYFAKHKWGN TTLRDLLVEL EATSGRDLSQ WSQLWLETAG VNTLIPHVET DADGVITSAS
IEQTATTELP TLRPHRLAVG LYALEGESLV RTDSVEVDID GAGTELPQLV GKQKGDLLLV
NDQDLAYAKI RLDEQSLRTV LDHPRALTDS LPRALVLGAA WDMTRDAQMP ARDFVSLGLA
TLREETDSNL LRSLLGQVGV AAARYVAPQH REATLAEITS TLRGLAVSAA PGSDAQLQLV
QAFAAEASSD EDAAYLRALL DGTSTLAGLE VDTEMRWTLL TALAATGHAD EEMIAAEQQR
DATATGSERA ARARAARPTP EAKAEAWRLV VERDDAPNQT LRAIGIGFQT VHDLELLAPY
VEKFHNAIAD VWATRTTATA GSIATLMYPL PLADQGLLDA SEQWLTDHAD ASAGLRRVVA
ENRDSVRRAL AAQACDAARD
//
