ID F8EVF2_ZYMMT Unreviewed; 462 AA.
AC F8EVF2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:AEI37359.1};
DE EC=3.4.11.1 {ECO:0000313|EMBL:AEI37359.1};
GN OrderedLocusNames=Zymop_0456 {ECO:0000313|EMBL:AEI37359.1};
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI37359.1, ECO:0000313|Proteomes:UP000000491};
RN [1] {ECO:0000313|EMBL:AEI37359.1, ECO:0000313|Proteomes:UP000000491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC NCIMB 11200 / NRRL B-4491 / Barker I
RC {ECO:0000313|Proteomes:UP000000491};
RX PubMed=21742897; DOI=10.1128/JB.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(2011).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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; CP002865; AEI37359.1; -; Genomic_DNA.
DR RefSeq; WP_013933758.1; NC_015709.1.
DR AlphaFoldDB; F8EVF2; -.
DR STRING; 579138.Zymop_0456; -.
DR KEGG; zmp:Zymop_0456; -.
DR PATRIC; fig|579138.3.peg.477; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_1_5; -.
DR Proteomes; UP000000491; Chromosome.
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:AEI37359.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEI37359.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 309..316
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 462 AA; 49814 MW; 784B143AA7943CDB CRC64;
MRAFQSLLAT DQGQPAQAIE TVTVEQFEKI IADKDPNFNA AAKLSQFTGQ PGSCLILPAT
EKQAWQIYVG VSEKHTVWDL AKAASFLPEG CYRLRAKNSP LLALGWLLAQ HHFDRYRSKS
SLRPECQLLI DADQNIVDEI IAQAEAVAMV RDLVDTPACD CGPEDLQHKV KEIAESFHAK
VTVTKGEDLE KGYPMIAAVG RAAAPHRMPR LIELHWGDPD KPKIALVGKG VCFDSGGLDI
KPSSSMLLMK KDMGGAAHAL ALAYLVMALK LPVHLHLLIP AVENAVSGDA MRPGDILNSR
KGTTVEIGNT DAEGRLVLAD ALTKASESRP ELIIDFATLT GAARVALGPD LPALFSNDDA
LAHALADAGK SVDDPLWRLP LWSDYLSILK STIADINNAG AGGMAGAITA ALFLQEFISD
QVKWAHFDTF AWQPVAKAGR PKGGAAYGLL ASWKMLKDRF SE
//
