ID A0A258Z065_9PROT Unreviewed; 434 AA.
AC A0A258Z065;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OYZ58352.1};
GN ORFNames=B7Y21_03530 {ECO:0000313|EMBL:OYZ58352.1};
OS Hydrogenophilales bacterium 16-61-112.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970519 {ECO:0000313|EMBL:OYZ58352.1, ECO:0000313|Proteomes:UP000216368};
RN [1] {ECO:0000313|EMBL:OYZ58352.1, ECO:0000313|Proteomes:UP000216368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-61-112 {ECO:0000313|EMBL:OYZ58352.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYZ58352.1}.
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DR EMBL; NCHD01000013; OYZ58352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258Z065; -.
DR Proteomes; UP000216368; Unassembled WGS sequence.
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; 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:SF9; XAA-PRO AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43226; 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:OYZ58352.1};
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}.
FT DOMAIN 3..135
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 434 AA; 48462 MW; F2159167003DD837 CRC64;
MQPDSAIYRA RRQRVLDEMG EGVMIIATAP EVPRNRDTHY PYRHDSYFYW LTGFNEPEAV
VVLVGGKQPR HILFCRERNE EREIWDGFRY GPAAAREIFA FDDAFTYDVL DAELPKLLEN
QPLLAYIIGR DAAWDTQMMS WLNTVRSKAR SGVHAPNRMV DARIWLDEMR LVKDGHELAL
MRRAAEISTG AHRAAMRATR PGGHEYEIEA ELLSAFRRGG AEAPAYTSIV ASGANACVLH
YVFNNKPLKD GDLLLIDAAA EFGSYAADIT RTFPVNGTFS AAQRDAYELV LAAQAAAIAA
VRPGATWIAP HEAAVRVLTQ GMVDLKLLAG EVDGLIEANA YSRFYMHRTG HWLGMDVHDA
GEYKLHGEWR QLQPGMTLTV EPGLYIRPAD DVPEAFWNIG IRIEDDVAVS ATGCEVLTSP
PKTVADIEDW MRGE
//
