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Database: UniProt
Entry: V8CER7_9HELI
LinkDB: V8CER7_9HELI
Original site: V8CER7_9HELI 
ID   V8CER7_9HELI            Unreviewed;       455 AA.
AC   V8CER7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:ETD25231.1};
GN   ORFNames=HMPREF2086_00566 {ECO:0000313|EMBL:ETD25231.1};
OS   Helicobacter macacae MIT 99-5501.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD25231.1, ECO:0000313|Proteomes:UP000018731};
RN   [1] {ECO:0000313|EMBL:ETD25231.1, ECO:0000313|Proteomes:UP000018731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD25231.1,
RC   ECO:0000313|Proteomes:UP000018731};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:ETD25231.1}.
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DR   EMBL; AZJI01000001; ETD25231.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8CER7; -.
DR   STRING; 1357400.HMPREF2086_00566; -.
DR   MEROPS; M20.A21; -.
DR   PATRIC; fig|1357400.3.peg.783; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_4_0_7; -.
DR   OrthoDB; 5486471at2; -.
DR   Proteomes; UP000018731; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 2.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018731}.
FT   DOMAIN          249..334
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   455 AA;  49178 MW;  479E1C9730217D29 CRC64;
     MPPKNQSDCK NIPQKSCQKD FQQSCIELLC ELIKKPSITP QECGIYQIIE SKLDEVGGFR
     FLRFDKGGVK NLFAYKVLEK KSSAKSSGDL SADSNINLSA KSSTISSDSI RHFCFMGHID
     VVPAGGNWSV EPFGAAVREG KIYGRGAQDM KAGVAAFVSA VVDFAREIEA SKIKARGVGE
     ASKAMEASEA KSQNDLPILS ILLTSDEEGE GIYGTRYALS ELQKLDLLPT HAIVAEPTCD
     EEFGDMIKVG RRGSINGSLK IIGKQGHAAY PQKCLNPIEA LSVALPLIAG VKLDEGNEYF
     SPSTLVATDI RGGLEVCNVT PSDVTLRFNL RNSTLFGLGD LEVHFGRIVE MIEHKVEGVK
     CELTLSQSSK PFLSNANSTL IKSLAKSVEK ITHITPTLGT GGGTSDARFA KEFGIEVAEF
     GVKNDKIHSV DECVEIAQVV GLYEVFLDFL KNEIA
//
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