ID A0A1N6TMX8_9FLAO Unreviewed; 537 AA.
AC A0A1N6TMX8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peptidase family M1 {ECO:0000313|EMBL:SIQ54436.1};
GN ORFNames=SAMN05421797_10222 {ECO:0000313|EMBL:SIQ54436.1};
OS Maribacter ulvicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=228959 {ECO:0000313|EMBL:SIQ54436.1, ECO:0000313|Proteomes:UP000186953};
RN [1] {ECO:0000313|EMBL:SIQ54436.1, ECO:0000313|Proteomes:UP000186953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15366 {ECO:0000313|EMBL:SIQ54436.1,
RC ECO:0000313|Proteomes:UP000186953};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTMA01000002; SIQ54436.1; -; Genomic_DNA.
DR RefSeq; WP_076548025.1; NZ_FTMA01000002.1.
DR AlphaFoldDB; A0A1N6TMX8; -.
DR STRING; 228959.SAMN05421797_10222; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000186953; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
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; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012975401"
FT DOMAIN 260..461
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 537 AA; 62338 MW; 50F6098C78266D44 CRC64;
MKKLAVALVL IVCSVSHAQT FTEQDTLRGS ITPEREWWDL NYYHLDIEVD PNDKFISGSN
TIRYKVLEPH QVLQVDLQPP LTIEKVTQDG QELKVVNNIN AHFIQLTKPQ NVGDFNEVVV
TYSGHPKEGV KAPWDGGFSW KKDENGKDFV ATSCQGLGAS VWWPNKDHMY DEVDSMLISV
KAPKGLMNIS NGRLRSVEKE SNTYNWFVSN PINNYGVNVN IGDYVHFNEI YQGEKGGLDM
DYYVLKDNLD KAKEHFIDAP KMMEAFEHWF GPYPFYEDSF KLVEVPYLGM EHQSSVTYGN
QYQKGYLGRD VSGTGWGLKF DFIIIHEAGH EWFANNITYK DAADMWVHEG FTSYSENLFL
DYHYGTEAAN EYVQGVRKNI KNDKPIIGTY NVNHEGSRDM YYKGANILHT LRQVVNDDRK
WRTILRRLNS EFYHKTVTTE QIERFIALEM KRDLKPFFNQ YLRTTKIPVF DYKLKGNKLM
YRFSNTVDDF TMPVKVYVND TPIWIEPTSK WQTKKITGSL GSLQVDPNYY IESKNKI
//