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Database: UniProt
Entry: B8J7Y8_ANAD2
LinkDB: B8J7Y8_ANAD2
Original site: B8J7Y8_ANAD2 
ID   B8J7Y8_ANAD2            Unreviewed;       520 AA.
AC   B8J7Y8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:ACL63480.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=A2cp1_0121 {ECO:0000313|EMBL:ACL63480.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL63480.1, ECO:0000313|Proteomes:UP000007089};
RN   [1] {ECO:0000313|Proteomes:UP000007089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001359; ACL63480.1; -; Genomic_DNA.
DR   RefSeq; WP_012631567.1; NC_011891.1.
DR   AlphaFoldDB; B8J7Y8; -.
DR   KEGG; acp:A2cp1_0121; -.
DR   HOGENOM; CLU_009902_6_1_7; -.
DR   Proteomes; UP000007089; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..520
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002875196"
FT   DOMAIN          82..186
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          233..406
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          23..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..520
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  54152 MW;  EE6633EC4F26EC2C CRC64;
     MTRSLRLLAV LLAAALGCAG SRPAPAPAAP AAAPQPQAAA APAGADRTQV PAAGEAPELH
     LPRQQHFALA NGLRVRLVEH RRLPIVALNL VVRAGAVNDP AGLPGLASFT ASMLTEGGTR
     SRTATRLSDE VGFLGASLGA GTGQDAASLS GSSLSRHLPK LLDLFADVAM NPAFRAKDFA
     RVQDQRKVTL LQQRDQPATI AGKAFLKAYW GEGHPYGHYV LGDEASVAAT RPADLAAFHA
     RFWRPANAEL VVVGDVSEAE LRPLLERTLG KWPAGTAAAA PRAPAPAAPH VTLLLDKPDA
     PQTLVMLGMP GLARASPDYV AATVAFQVLG GGMSSRLFRT LREEKGYTYG MGAGADARRL
     GGVSIVHGNV KAEVTGAALG DLLGEIRKLR DQPVGDAELA DARNALVRSL PADFATVGGI
     AGRVAELVIH GLPDDYWNGY ADAVRDVAPA DVQRIAERYL DPARATLVLV GTPAAVRPQL
     EGLAIGKVEV RPVPGAAPVR APPRSPRVRT QRPPTSSPAP
//
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