ID F5HNH9_BORGR Unreviewed; 190 AA.
AC F5HNH9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
DE Flags: Fragment;
GN Name=pepX {ECO:0000313|EMBL:BAK23533.1};
OS Borreliella garinii (Borrelia garinii).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=29519 {ECO:0000313|EMBL:BAK23533.1};
RN [1] {ECO:0000313|EMBL:BAK23533.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HP3 {ECO:0000313|EMBL:BAK23517.1}, HT59
RC {ECO:0000313|EMBL:BAK23533.1}, and NT31 {ECO:0000313|EMBL:BAK23597.1};
RX PubMed=21411595; DOI=10.1128/JCM.02544-10;
RA Takano A., Nakao M., Masuzawa T., Takada N., Yano Y., Ishiguro F.,
RA Fujita H., Ito T., Ma X., Oikawa Y., Kawamori F., Kumagai K., Mikami T.,
RA Hanaoka N., Ando S., Honda N., Taylor K., Tsubota T., Konnai S.,
RA Watanabe H., Ohnishi M., Kawabata H.;
RT "Multilocus Sequence Typing Implicates Rodents as the Main Reservoir Host
RT of Human-Pathogenic Borrelia garinii in Japan.";
RL J. Clin. Microbiol. 49:2035-2039(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU004387};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; AB555785; BAK23517.1; -; Genomic_DNA.
DR EMBL; AB555801; BAK23533.1; -; Genomic_DNA.
DR EMBL; AB555865; BAK23597.1; -; Genomic_DNA.
DR AlphaFoldDB; F5HNH9; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAK23533.1"
FT NON_TER 190
FT /evidence="ECO:0000313|EMBL:BAK23533.1"
SQ SEQUENCE 190 AA; 21096 MW; D768101AA332CE60 CRC64;
YNTHDNLTVI NSTKKTIKDN ILEQLGIEYE NFLSCDLIFT ESQPSKIIGT EGEFLASKNL
DNKSGCHAIM DSYIHTSNNK NKIAVFFDNE EVGSLTSRGA DSNLLSEVLE RIDLALNLTR
EEHLIKTNKS FNISIDSVHG IHPGYASKHD PNYQATLSKG VVVKNSANFR YATTSTGFAK
LKNLAIKNNI
//
