ID   Q39R85_GEOMG            Unreviewed;       374 AA.
AC   Q39R85;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Leucyl aminopeptidase-related protein {ECO:0000313|EMBL:ABB33239.1};
GN   OrderedLocusNames=Gmet_3024 {ECO:0000313|EMBL:ABB33239.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB33239.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB33239.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB33239.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
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DR   EMBL; CP000148; ABB33239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q39R85; -.
DR   STRING; 269799.Gmet_3024; -.
DR   KEGG; gme:Gmet_3024; -.
DR   eggNOG; COG2309; Bacteria.
DR   HOGENOM; CLU_062630_0_0_7; -.
DR   Proteomes; UP000007073; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:ABB33239.1};
KW   Hydrolase {ECO:0000313|EMBL:ABB33239.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:ABB33239.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007073}.
SQ   SEQUENCE   374 AA;  40882 MW;  C35635C21938493E CRC64;
     MYQDAFRSLF EINMGIRSGE RVLVFSDTIR IDEAPIPSER NRRERLLQVA EEAARFAETT
     YGRTDFVSFP ATAASGAEPP ETLWRSAFGN GIVDTLAAEG ILPRLLAKEA TADDVERSRE
     LILASRRDVV DVVVALANNS TSHTRFRSLV NAAGGRFASL PHFDPEMFFT SMQVDWHALA
     ERTKQLAAAV NEATEILIET PNGTRMRIGK AGRQAEGDDG LLTAPGSFGN LPAGEVYLAP
     LEGTSEGVMV LEYGPTRKLS SSVELIVRNG IVTDIRGDEP HREWLERRFA ENGKNRNIAE
     LGIGTNDRAT RPDNILEAEK ILGTIHIALG DNSGFGGTVQ TPFHEDYVFY RPTLTAVAAN
     GSPTVLLRDG TLLL
//