ID S3J1B8_9ENTR Unreviewed; 438 AA.
AC S3J1B8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Aminopeptidase P domain protein {ECO:0000313|EMBL:EPF13712.1};
GN ORFNames=HMPREF0201_03903 {ECO:0000313|EMBL:EPF13712.1};
OS Cedecea davisae DSM 4568.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cedecea.
OX NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF13712.1, ECO:0000313|Proteomes:UP000014585};
RN [1] {ECO:0000313|EMBL:EPF13712.1, ECO:0000313|Proteomes:UP000014585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF13712.1,
RC ECO:0000313|Proteomes:UP000014585};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2013) 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:EPF13712.1}.
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DR EMBL; ATDT01000033; EPF13712.1; -; Genomic_DNA.
DR RefSeq; WP_016538115.1; NZ_KE161030.1.
DR AlphaFoldDB; S3J1B8; -.
DR STRING; 566551.HMPREF0201_03903; -.
DR PATRIC; fig|566551.4.peg.3560; -.
DR HOGENOM; CLU_017266_1_0_6; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000014585; 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:EPF13712.1};
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..438
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004510223"
FT DOMAIN 1..136
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 438 AA; 48854 MW; E3374D94F7E8AE4D CRC64;
MNQQEFLRRR QALLAKMAPA SAAIIFAAPE VTRNADSEYP YRQNSDFWYF TGFNEPEAAL
VLIKSDASHN HSVLFNRVRD KNAEIWSGRR LGQENAPQKL GVDRALAFAE IGEQLHLLLN
GLDVVYHAQG EYDYADNLVF AALDKLRRGS RQNLSAPASL TDWRPTVHEL RLFKSEEEIA
VMRRAGEISA LGHTRAMQTC RPGMFEYQLE GEIHHEFNRH GARYPSYTTI VGSGENGCIL
HYTENESQMR DGDLVLIDAG CEYQSYAGDI TRTFPVNGKF SPAQRAVYDI VLESLETSLK
LYRPGTTMQA VTAEVVRIMV KGLVKLGILK GDVEKLIADN AHRAFFMHGL SHWLGLDVHD
VGFYGPDRSR VLEPGMVITV EPGLYIAPDA DVPAQYRGIG IRIEDDIVIT ADGNENLTAS
VVKSADDIEA LMAAARQQ
//
