ID A0A172TG39_9BACL Unreviewed; 679 AA.
AC A0A172TG39;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=EnpEP protein {ECO:0000313|EMBL:ANE45922.1};
GN ORFNames=SY83_06035 {ECO:0000313|EMBL:ANE45922.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE45922.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE45922.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE45922.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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DR EMBL; CP011388; ANE45922.1; -; Genomic_DNA.
DR RefSeq; WP_068605189.1; NZ_CP011388.1.
DR AlphaFoldDB; A0A172TG39; -.
DR STRING; 1178515.SY83_06035; -.
DR KEGG; pswu:SY83_06035; -.
DR PATRIC; fig|1178515.4.peg.1207; -.
DR OrthoDB; 9814383at2; -.
DR Proteomes; UP000076927; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09604; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000076927};
KW Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 357..552
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 32..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 493
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 679 AA; 76516 MW; 06DC4A19A68EC33B CRC64;
MNHRLTLLLL PLLIIIALIG IVLYDPAEPS RSALSEVKPS GKGANANKSK QQPKAKPQPP
SAKAPSKGTS APDLPVVKKP EPLSKRVVEY HIHAKWNPAN KQINGTQTLT WTNPGKNAVS
EMYFHLYPNA FESMDTTFMK ESGGKLRSDQ MQAGSFGFMN ITAMKTAEGT NLLPRLQPVQ
PDDGNKNDRT LVKLRLPEPV PPKGSITLRM AFEVQLPHTF ARMGYAGDFV MAGQWFPKAA
AYELAGTRGR SAEGWNAHQY HGNSEFYSDF GIYNVKVAVP SNYVVAATGF QTKPTADKNG
IRTYQFYADD VHDFAWSASP HFVYAEEPFS APNVPGVRIK LYLDPKHKDL QDRYFHAAKS
ALTEYSKWYG QYPYSTLSIV VPPEEGNGAG GMEYPTLVTG FGASTEDPGL ELERVVVHEI
AHQYWYGIVA SNEFEEAWLD EGFASYSEDK VMEKEYGVAP NLPVESSYIT SPAPLKQLSW
KYNSHNHYAE NVYTRAKLVL LGIEKEIGQK AMSRVIRTYF AKWKYKHPST SDFQAVLEQI
TKKDWDRYFN QYVYGNMMAD YAVEDIRTER VRQNGNTVYE HRVYIRKHGA DFSKIPIVFQ
FEDGTSMKKM WNGTEALTEY KITNASPLAW VAIDPQYTIV VENKHINNFM KADVATDSNI
RWNLSITKIV EALIGSLAW
//
