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Database: UniProt
Entry: W8RR06_9RHOB
LinkDB: W8RR06_9RHOB
Original site: W8RR06_9RHOB 
ID   W8RR06_9RHOB            Unreviewed;       470 AA.
AC   W8RR06;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Peptidase B {ECO:0000313|EMBL:AHM03604.1};
DE            EC=3.4.11.23 {ECO:0000313|EMBL:AHM03604.1};
GN   ORFNames=roselon_01213 {ECO:0000313|EMBL:AHM03604.1};
OS   Roseibacterium elongatum DSM 19469.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseibacterium.
OX   NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM03604.1, ECO:0000313|Proteomes:UP000019593};
RN   [1] {ECO:0000313|EMBL:AHM03604.1, ECO:0000313|Proteomes:UP000019593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP004372; AHM03604.1; -; Genomic_DNA.
DR   AlphaFoldDB; W8RR06; -.
DR   STRING; 1294273.roselon_01213; -.
DR   KEGG; red:roselon_01213; -.
DR   PATRIC; fig|1294273.3.peg.1191; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_2_1_5; -.
DR   Proteomes; UP000019593; 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; SSF52949; Macro domain-like; 1.
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:AHM03604.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHM03604.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019593}.
FT   DOMAIN          317..324
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   470 AA;  49153 MW;  2B6C2722FF6691D9 CRC64;
     MRDLPMGALM PLAFSAPVDG AIPILLIAPE ACDDAMTNLP DNAAAWAKFH RFSGGLGEVC
     VLPGPAGGPE TVLIGLGGAE DRARQRFAIG AAIARLPEGD YRIETLPDAA DAEEIALGYL
     LSLYRFDRYR AQSPASARLA APEGLDAARL ERIATAEAMT RDLVNTPAED MGPDALEAAL
     RDLAAEFGAE VHATHGDSLL DANLPLIHTV GRASDEAPRL LDMTWGDGGP SLTLVGKGVC
     FDTGGLNLKP GASMALMKKD MGGAANVLGL ARMIMSEGLK LRLRVLIPAV ENAVSGNAFR
     PGDISTARNG MTVEINNTDA EGRLVLADAL CLAAEDNPDL LISMATLTGA ARVAVGPDIA
     PFFTDDEGLA AALSRCAVEV ADPVWRLPFH TPYEAMIEPG IADLDNAPKG GMAGAITAAL
     FLRRFAAPAP RYAHFDIYAW QPSAAPARPK GGVGQGIRAL FEALPEVLQP
//
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