ID A0A2S8B829_9SPHN Unreviewed; 899 AA.
AC A0A2S8B829;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=CVO77_08965 {ECO:0000313|EMBL:PQM28564.1};
OS Sphingopyxis lindanitolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=2054227 {ECO:0000313|EMBL:PQM28564.1, ECO:0000313|Proteomes:UP000238954};
RN [1] {ECO:0000313|Proteomes:UP000238954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS5A3p {ECO:0000313|Proteomes:UP000238954};
RA Kaminski M.A.;
RT "The complete genome sequence of Sphingopyxis pomeranensis sp. nov. strain
RT WS5A3p.";
RL Submitted (NOV-2017) 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:PQM28564.1}.
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DR EMBL; PHFW01000002; PQM28564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8B829; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000238954; Chromosome.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000238954};
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..899
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015466244"
FT DOMAIN 58..241
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 276..488
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 572..863
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
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 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 435
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 899 AA; 95541 MW; F8F4902E24652564 CRC64;
MKISTRHLLV AAVSSLGLAA CAAQPGVAPP APAALMPAPT GAPLDASVPS QLPRIARPLH
YDISVTPDAK ALSFTGEAGI DLELYAPSTT IVMNALDLTF TDAALTGPDG KPVLLTAATD
AEAQTVTFTA PAPIAPGTYR LDARYSGVIN TQANGLFALD YPDKTTGADT RGLFTQFEAS
DARRFIPSFD EPSYKATFSL SAIVPADDLV VSNMPAANET PVEGGRKKVT FQISPKMSSY
LLFFATGPFE RLAKKSESGA EVGIVSPRGS GEQARFALDS LAPLLTYYAD YFGQPYPLPK
LDNVAGPGQS QFFGAMENWG AIFTFERILL DDPKITSDAT RQAIYAVQAH EVAHQWFGDL
VTMAWWDDLW LNEGFASWME TKASDHFHPD WQPLLDRVGG REAAMGLDAF ATTHPIVQTI
RTVEDSNQAF DAITYQKGEA VITMLEAYAG ADKWRGGLRA YVAQHRYGNT RTDDLWRAVE
AAGATGLTGI AHDFTNQPGI PLLRVGAATC AGGTTTVSLT QSEFSRDRKD SIDAEGRRWR
VPVLARAGDG AVSRQVVTGG AGTLTLPGCR PVLINAGQAG YYRTLYSPAA LAALRGRFAS
LAPIDQLGLL GDNFALAYAG YQPMGAALDL LAAAPRDANP KLIGDVASRY EALYTLFDDQ
PAVQKQITML GSAALAPAMR RLGFDARPGE PALDGVLRSE LLGALGTIGD AKIRAEALRR
FALLDRDPAA LDGPLKSRWL GIVAANAGAA EWDRLRALAK GSKSAVERSA FYTLLGNAKD
AKLAKRALDL ALTDEPGKTT SAAIIGTVAR RHAEMAVAFA QANQAAVDAL IDASARARFL
AGLAASSTDP AMIATLEAIA APLSADVRKP YDKTIAALKE RRTSRPRIKG EVEGWLKGK
//
