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Database: UniProt
Entry: A0A0S7B9F0_9CHLR
LinkDB: A0A0S7B9F0_9CHLR
Original site: A0A0S7B9F0_9CHLR 
ID   A0A0S7B9F0_9CHLR        Unreviewed;       385 AA.
AC   A0A0S7B9F0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:GAP13991.1};
GN   ORFNames=LARV_01750 {ECO:0000313|EMBL:GAP13991.1};
OS   Longilinea arvoryzae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Longilinea.
OX   NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP13991.1};
RN   [1] {ECO:0000313|EMBL:GAP13991.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOME-1 {ECO:0000313|EMBL:GAP13991.1};
RA   Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT   "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT   caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT   saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT   Members of the Anaerolineaceae (Chloroflexi).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; DF967972; GAP13991.1; -; Genomic_DNA.
DR   RefSeq; WP_075073283.1; NZ_DF967972.1.
DR   AlphaFoldDB; A0A0S7B9F0; -.
DR   STRING; 360412.LARV_01750; -.
DR   Proteomes; UP000055060; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR001261; ArgE/DapE_CS.
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   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055060};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          169..272
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   385 AA;  41623 MW;  510FA1BE5CDB9453 CRC64;
     MSSEAFETEL VDFTQAIIRV NSLSGKEEAV GGLIVEKMKA LGYDSAQVDR YGNVIGIRRG
     KHPGPTILFD GHMDVVPVTT PEAWSSDPFG AQIREGKIWG RGASDMKGPL AAAVVAIGHV
     PAEEIHGTIV VSGSVCEEYH EGAAVQKVVE QVLPDFVVIC EPNGNRLGIG QKGRAGLWLE
     VSGKPAHSSV PHLGENAIYK AVPIIERLRR MPLPCDPFLG NGVMELIDAI SGPYPSRSTL
     PVSFRMRYDR RLMQGETMDT VLESIHEALR DLSDWQVGFS MVHMDTWTGD LLEGPDFHPG
     WLMEETSPWV VKAGRGLTEA GVEPVFDAAR FCTNGSYTAG EAKLPTIIFG PSSGMLAHCI
     DENIGIDELC LGAQGYMGLA KNLGR
//
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