ID A0A1Q5PQV0_9ACTO Unreviewed; 511 AA.
AC A0A1Q5PQV0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OKL49780.1};
GN ORFNames=BSR29_02195 {ECO:0000313|EMBL:OKL49780.1};
OS Boudabousia liubingyangii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Boudabousia.
OX NCBI_TaxID=1921764 {ECO:0000313|EMBL:OKL49780.1, ECO:0000313|Proteomes:UP000186785};
RN [1] {ECO:0000313|EMBL:OKL49780.1, ECO:0000313|Proteomes:UP000186785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VUL4_2 {ECO:0000313|EMBL:OKL49780.1,
RC ECO:0000313|Proteomes:UP000186785};
RA Meng X.;
RT "Actinomyces gypaetusis sp. nov. isolated from the vulture Gypaetus
RT barbatus in Qinghai Tibet Plateau China.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766, ECO:0000256|RuleBase:RU000590}.
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:OKL49780.1}.
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DR EMBL; MQSV01000001; OKL49780.1; -; Genomic_DNA.
DR RefSeq; WP_073708664.1; NZ_MQSV01000001.1.
DR AlphaFoldDB; A0A1Q5PQV0; -.
DR STRING; 1921764.BSR28_00290; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000186785; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OKL49780.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186785}.
FT DOMAIN 51..200
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 56242 MW; D06821C34211D7C2 CRC64;
MSDSKDTAKK DQKEYATGNE NRAPSPFPQA FRDFIGSNWG PREDAGVTRQ AVADYLPARH
EAVGANFPGQ RLVLPAGTYK QRSNDCDYRF RAHSAFAHLT GLGGELEPDA VLVLEPQPEG
SAQSHKPVLY FQPRASRSSE QFYADSTYGE FWVGPRPSLE EMETMTGLDC APIDTLGDAL
AKDAGLVNLR VVPGVDTKVE SLVNEVRQQA GLPFGKDATA EDKDFERVLS ELRLTKDEHE
VAELQHAVDV TYAGFEGIIK SLPRAVGHHR GERVIEGAFG AVAREEGNGL GYDTIAASGN
HANTLHWIDN DGPVRPGDLV LVDAGCEVDS LYTADITRTL PVDGKFTEAQ AELYNAVLEA
CEAALEAANQ PGAKFRHLHE AAIKVLVKHL DAWGILPVSQ EESLSPQGQQ HRRWMPHGTS
HHLGLDVHDC AQARREMYVE AELEPGMCFT IEPALYFRSD DLLAPERFRG MGVRIEDDCL
VQADGKVIRL SEDIPRTVED VEAWIERVQN S
//
