ID A0A0S8H990_9BACE Unreviewed; 477 AA.
AC A0A0S8H990;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M17 {ECO:0000313|EMBL:KPK81060.1};
GN ORFNames=AMS27_15770 {ECO:0000313|EMBL:KPK81060.1};
OS Bacteroides sp. SM23_62_1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK81060.1, ECO:0000313|Proteomes:UP000051265};
RN [1] {ECO:0000313|EMBL:KPK81060.1, ECO:0000313|Proteomes:UP000051265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK81060.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK81060.1}.
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DR EMBL; LJUQ01000212; KPK81060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8H990; -.
DR PATRIC; fig|1703353.3.peg.1921; -.
DR Proteomes; UP000051265; 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 PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 326..333
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 477 AA; 53106 MW; 1F5D02A9E33482D4 CRC64;
MNISLLKKIP DNEDLIILGK QDSPFDMYLQ NNEEKGYLRH ALGDKKKQII INQYKRWIFL
HIIEENKKPG HQVLEEIRKG GKKLLQAVND KKIKQVCIVD LSADASYFYA FIEGIALSNY
QFLKYLTKTS EEVNSLNTLH IYSNVLKKKQ VEELIHLIHG VYLARDLVNE PLSYLTALQL
SKEIEKIGKD AGFSVEVYHK KKIESLRMGG LLAVNKGSID PPTFSILTWK PQNAKNKKPY
VLVGKGIVYD TGGLSLKPTF ESMDYMKCDM AGAAAVAGAI YILARTHTPL WVVGLIPATD
NRPDGNAYAP GDIIRMYDGT TVEVLNTDAE GRMILADALS WAKKYNPELV IDIATLTGAA
QAAIGNYGIV AMGNAGNEIF DIMKSSGEAV YERIAHFPFW DDYAELLKSD IADIKNVGGK
YAGAITGGKF LEHFTDYPFI HLDIAGPAYN KIKDSYRGKG ASGVGVRLLF NFLKRRA
//
