ID I4WL24_9GAMM Unreviewed; 402 AA.
AC I4WL24;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Leucine aminopeptidase {ECO:0000313|EMBL:EIM00166.1};
DE Flags: Fragment;
GN ORFNames=UU5_02372 {ECO:0000313|EMBL:EIM00166.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIM00166.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIM00166.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIM00166.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIM00166.1}.
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DR EMBL; AJXS01000061; EIM00166.1; -; Genomic_DNA.
DR RefSeq; WP_008208701.1; NZ_AJXS01000061.1.
DR AlphaFoldDB; I4WL24; -.
DR PATRIC; fig|1162282.3.peg.461; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR048816; Peptidase_M17_N_1.
DR PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF21337; Peptidase_M17_N_1; 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:EIM00166.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 248..255
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIM00166.1"
SQ SEQUENCE 402 AA; 43389 MW; C72123BF5906EF41 CRC64;
NGKLERVLVG VDATQPLAAL AALPATLPEG TYQLAEDGVA LDAQQAALGW ALGAYQFTRY
RKAKREPATL SVDAAVFAAV QPLVDATALV RDLVNTPTED MGPEQIGDAI KTLGKTHKAK
VRDWVGDELL KANFPTIHAV GRASHREPRL IELSWGKLDD PKLVLVGKGV CFDTGGLDLK
SADGMRWMKK DMGGSAHAIA LAGLVMQARL PVRLTLLVPA VENSVAGNAM RPGEVIVTRA
GHSVEIDNTD AEGRLILCDA LAYGAEQKPD LMVDFATLTG AARVALGPDL PALFSNDDAL
AEATLAAGRA NNDPLWRLPL WRPYFKMLDS YLADFANAGP SRHAGAITAA LYLERFVPDA
QRWMHLDTYA WNDVDRHGRP RGGEAMGLRA VFAMLEQRYR KS
//
