ID A0A1M3FZS9_9SPHI Unreviewed; 653 AA.
AC A0A1M3FZS9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase M1 {ECO:0000313|EMBL:OJW32922.1};
GN ORFNames=BGO54_14810 {ECO:0000313|EMBL:OJW32922.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW32922.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW32922.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW32922.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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};
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:OJW32922.1}.
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DR EMBL; MKTY01000020; OJW32922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3FZS9; -.
DR STRING; 1895839.BGO54_14810; -.
DR Proteomes; UP000184358; Unassembled WGS sequence.
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; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..653
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012160171"
FT DOMAIN 367..552
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 492
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 653 AA; 74002 MW; 24CF9BC04048AA58 CRC64;
MKCIAAAITA SIITLLASGQ SAFDAKEAFN PHFYPYPGNE MRSAGGEPGP GYWQNQASYR
INCTLDTGQK RITGSVDIEY VNNSPDNLRF LWLQLDQNIY KKDSRGSATT TEAGGRWAND
GYTSGYIITA VEAESAGGKY AARYLINDTR MQVWLQEPLQ AKGGKIKLSI PFAFTIPEYG
TDRMGLLNSQ HGWIYQIAQW FPRLCVYDDI QGWNVDPYLG AGEFFLEYGH IEYAITAPAN
LLVVGSGTLL NPSECFNAEE LVRYNQAKES DKTILIRSLK DVTAQVRNSR MGTITWKFSI
ENARDVAWAA SGAFILDGAR INLPSGKRAL ALSAYPAESA REKKEEDWRK STEMVKASIE
YYSGKWYEYP YTTAVNVAGS VGGMEYPGIV FCSYSSTGSS LWNVTDHEFG HTWFPMIVGS
NERKYAWMDE GFNTFINDLS TEAFRNGVYN NANLFSNPSL PFMIQATFGD EMDAMFTSPD
VIQQQNLGIA AYMKPAQMLH ALRDVVLGPE RFDAAFKEYI RRWAFKHPTP WDFFHTMENV
GGEDLAWFWR GWIFNSWKLD QAVKEVKYVK NNPGNGAEIT IENKEKMPMP VDLLIKESNG
KEHRLLLPVE VWQRGATWTI HLQVTSEIKE IIIDPDKKLP DWNRENNRWK RAF
//