ID I3IDH4_9GAMM Unreviewed; 437 AA.
AC I3IDH4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aminopeptidase P II {ECO:0000313|EMBL:EIK46109.1};
DE EC=3.4.11.9 {ECO:0000313|EMBL:EIK46109.1};
GN Name=pepP {ECO:0000313|EMBL:EIK46109.1};
GN ORFNames=O59_000130 {ECO:0000313|EMBL:EIK46109.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK46109.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK46109.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK46109.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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}.
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:EIK46109.1}.
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DR EMBL; AICM01000001; EIK46109.1; -; Genomic_DNA.
DR RefSeq; WP_007638436.1; NZ_JH668200.1.
DR AlphaFoldDB; I3IDH4; -.
DR STRING; 1134474.O59_000130; -.
DR PATRIC; fig|1134474.3.peg.128; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_1_0_6; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000003395; 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; IPR001714; Pept_M24_MAP.
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 PRINTS; PR00599; MAPEPTIDASE.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:EIK46109.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EIK46109.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 3..137
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 437 AA; 49130 MW; 52D3D31BDE1B6AA9 CRC64;
MRISKTEFAR RRKQLMAMME PNSIAIVPAA PERTRSRDTE HHYRQDSDFL YLSGFEEPSA
VLVLIPGREH GEFVLFVRER NREREIWDGY RAGPEGACSE FDADDAFPID DIDDILPGLL
EGKQRVYYAM GKDADFDKHV MDWVNTIRAK VRSGATPPGE FLDLSHFLNE LRLFKSAAEL
RVMKEAGEIS ARAHVRAMKA SKAGVMEYQL EAEILHEFQM SGARFPAYNT IVGGGKNGCI
LHYIENSAPL KNGDLVLIDA GCELDYYAAD ITRTFPVNGK FSPEQKALYE ICLQAQLDAI
AMCKPGNHWN DPHEATVRVI TEGLVKIGLL EGDVNELIKS EAYKEFYMHR AGHWLGMDVH
DVGDYKVGGE WRVLEPGMVL TVEPGIYVAP DNERVAKKWR GIGIRIEDDV VITKDGNEVL
TKDVPKTVAE IEALMAV
//
