ID   C1FQE6_CLOBJ            Unreviewed;       718 AA.
AC   C1FQE6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Putative membrane protein {ECO:0000313|EMBL:ACO87008.1};
GN   OrderedLocusNames=CLM_2349 {ECO:0000313|EMBL:ACO87008.1};
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO87008.1, ECO:0000313|Proteomes:UP000001374};
RN   [1] {ECO:0000313|EMBL:ACO87008.1, ECO:0000313|Proteomes:UP000001374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001581; ACO87008.1; -; Genomic_DNA.
DR   RefSeq; WP_012705640.1; NC_012563.1.
DR   AlphaFoldDB; C1FQE6; -.
DR   KEGG; cby:CLM_2349; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_023502_0_0_9; -.
DR   Proteomes; UP000001374; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   TRANSMEM        32..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          553..709
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        572
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        663
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         575
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         595
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   718 AA;  80737 MW;  4028A2926C3FA675 CRC64;
     MILTMLCPMA GYKLYNNGID GTLSGKFIGN PSIAGAVGGG ILFAILTLLE FDRVHKYEIE
     GLTNSIVSPL VLNVGRLLTI GIAATVTVSI TSVLYYPYTV TKMGNIFDIY TYLNSFFLLM
     LPSVLLSILA ASALYQIFYR VDLSMAAFIL LMLPNLIENL PIGNILHWIR PSVPAMSDYF
     SNTQIFRLMK HNRLFWFLIF GGLWLIGLLS VRCYGKRIFG SMLYNSRKVY IPLIAVAMIG
     GGCYAFINQP DVSLVSKEGI MEIINSSSKD SSDKVNKEIQ LLNSDLKISF DGSKGSLSGK
     AVYSLQNLSN SKQECKFTIN PGYNIHQIIV NDKKVTFKKL KDIRNNIIFN VPKEKNIKLT
     IEYEGRPKIL YFLSDFLLDT NISDKYIDLN RDFIPNIKVA NSKDNPELTC QLTMPSGLMP
     VVNPAQEDES GEEVANLTGD TTLLLADGDK KTWLVHLKGT RLSLMAGDYV MKQLGNEEMP
     IKLYYSSKHE DTMKNMSAEK VMKDTIDYCI SHYGKLNNVS KNSPLKIVEK TELFPGGLAL
     PNYSTIGGAC FNDENLSDKS KRASADETLA HELAHQWWGV HTVGSGGNNR NWSAEGLAVY
     TTYRVAKKTH GEEYAKKNYV DIWKARVKEN NNNFYTRHPE YLKILPQRYV QDIDGNDRVL
     RQYSKLPLQI LKASKLVGGE DKMDKILAEL YKNKSKTRIT WQDFLNACEL KGGELNLE
//