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Database: UniProt
Entry: B9NTZ4_9RHOB
LinkDB: B9NTZ4_9RHOB
Original site: B9NTZ4_9RHOB 
ID   B9NTZ4_9RHOB            Unreviewed;       460 AA.
AC   B9NTZ4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Cytosol aminopeptidase family protein {ECO:0000313|EMBL:EEE38247.1};
GN   ORFNames=RKLH11_2089 {ECO:0000313|EMBL:EEE38247.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE38247.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/jb.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT   Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL   J. Bacteriol. 193:5011-5012(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; DS999531; EEE38247.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9NTZ4; -.
DR   STRING; 467661.RKLH11_2089; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_2_1_5; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000005135; 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:EEE38247.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135}.
FT   DOMAIN          308..315
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   460 AA;  48338 MW;  3121F65C55011F1D CRC64;
     MTLSFASPSD PSLPLHVLAQ ADLDDWLAEQ PDHVQSWVAA NGFTGALGQA LVVPGPGGAP
     DCALAGYGST AKRARKRFPL AAAAEALPEG SYHIASGLPD DVREAECLGW LMTAYTYDRY
     AAQSLSKAAL VAPEGIDATR IEIMANAEAL IRDLVNTPAS DMGPRQLQHA VEALAKEYGA
     DCAVISGKAL LDQDFPLIHT VGRAAEQAPR LIEMNWGDHG PKLTLVGKGV CFDTGGLNLK
     PGASMGLMKK DMGGAANVLG LARMIMALGL KIRLRVLIPA VENAVAGNAF RPGDILTARN
     GLTVEINNTD AEGRLVLADA LALADEDDPD LLISMATLTG AARVAVGPDL APYYTDDDKA
     AAALSRAGQT AADPVWRMPF HEPYEAMIEP GIADLDNAPA GGFAGSITAA LFLRRFAGDS
     RYMHFDIYAW QRSKEPGRSK GGLGQGPRAL LAALPEILSL
//
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