ID Q836S5_ENTFA Unreviewed; 729 AA.
AC Q836S5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=6-aminohexanoate-cyclic-dimer hydrolase, putative {ECO:0000313|EMBL:AAO80836.1};
GN OrderedLocusNames=EF_1033 {ECO:0000313|EMBL:AAO80836.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO80836.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO80836.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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DR EMBL; AE016830; AAO80836.1; -; Genomic_DNA.
DR RefSeq; NP_814766.1; NC_004668.1.
DR AlphaFoldDB; Q836S5; -.
DR STRING; 226185.EF_1033; -.
DR EnsemblBacteria; AAO80836; AAO80836; EF_1033.
DR KEGG; efa:EF1033; -.
DR PATRIC; fig|226185.9.peg.966; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_12_1_9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895:SF180; AMIDASE AMIC-RELATED; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAO80836.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001415};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 706..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..540
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 78078 MW; F20F0FC302F7176F CRC64;
MLAQESILET TVQTETESVT TETSQTVANL ESETTSQTVM QEKESSSAIA ESSSGNAVAV
TTETTNEIQN SDTDGKAVSA ESVFSEADYK QATALELATL VREKKVTSEE LVKIALAITK
RENPTLNAVI TLREEAALTE AKALQDTGQP FLGVPLLLKG LGQSLKGESN TNGFGFLQDQ
VAGGTSTFVK ALQNAGFIII GQTNYPELGW KNISDSKLYG VSVNPWNPNH YSGGSSGGAG
ASVAAAFVPI ASGSDAGGSI RIPASWTGTV GLKPSRGVII GNSNSAKGQT VHFGLSRTVA
DTNALFETLL TKKDLPAGHL SQAQPIAYTT ESPAGTPISA EAKEAVAEAV AFLKDQGYTL
VEVKHPVDGE RLMKNYYTVA AGSAGIADFM ARQKLKRPLE RNDVELLTWA LFQTGKNITS
EETTAAWTDI ALQAQAMDEF YQQYPILLTP TTAATAPSID NPLLKPEHAA QMEKIDQLSP
AEQKQLIYDQ WLTAFTYTPF TQQANLFGHP ALSVPTYVSK EGLPLGIQFN SALNEDRTLL
QLGALFENNH KINQPHVEEP DKDKEPDTSG EPDKDKEPNA SGELDKDKDP DASGEPDKDK
DPDASGEPDK DKELDTSGEP DKDKETKTSE GPIEGKDQNQ NQNQNPDKSG KTTSESSLDN
SLNSSANQGT KSTESTHAFS DKNMIGKKEQ LPKKVLPKAG AEVPSTFWVV LGGAFLVTSG
TIYIRKTRK
//