ID A0A0W7U2B9_9GAMM Unreviewed; 424 AA.
AC A0A0W7U2B9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KUE80209.1};
GN ORFNames=ATO46_03415 {ECO:0000313|EMBL:KUE80209.1};
OS Aeromonas schubertii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=652 {ECO:0000313|EMBL:KUE80209.1, ECO:0000313|Proteomes:UP000054876};
RN [1] {ECO:0000313|EMBL:KUE80209.1, ECO:0000313|Proteomes:UP000054876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43700 {ECO:0000313|EMBL:KUE80209.1,
RC ECO:0000313|Proteomes:UP000054876};
RA Liu L., Li Q., Zhang F., Shi B.;
RT "Complete genome sequence of Aeromonas schubertii strain ATCC43700.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:KUE80209.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPUO01000012; KUE80209.1; -; Genomic_DNA.
DR RefSeq; WP_050665069.1; NZ_LPUO01000012.1.
DR AlphaFoldDB; A0A0W7U2B9; -.
DR STRING; 652.WL1483_812; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000054876; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KUE80209.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 269..276
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 424 AA; 45270 MW; DC30B81B07CF8464 CRC64;
MNVWLSRDPA APAWGEGALL SWHQEGIAIH LGSDPLGDIQ QGARRLCAQG IQQAALCGHW
EREQQWAFAQ GFQTPKAEVQ LQWATCEESD RAELEARWLC GRWVREMTNA TPEQIGPLEL
AVEAAAFITE LAPDRVSHRI LKGEALQQAG WTGIWSVGRG SAREPVLLEL DYNPTRDPKA
PVAAALVGKG ITFDSGGYSM KSSEGMLTMK CDMGGAAIVT GALGLAIARG LTKRVKLILC
CAENLVSGHA YKLGDILTYK NGTTVEIVNT DAEGRLVLAD GLQLAGESGA PLIIDAATLT
GAAVMALGGR YNALFGLDKP LVERARQVAD AEQEPAWPLP LERWHRGMCP SHYADTANSR
PVKGGGAGGA SNAAGFLSRF VPRDGEGWLH IDLAACFCDN GDSLWAPGAT TLGMRTVARL
LEQA
//
