ID I0JSX9_HALH3 Unreviewed; 395 AA.
AC I0JSX9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Aminoacylase {ECO:0000313|EMBL:CCG47251.1};
DE EC=3.5.1.14 {ECO:0000313|EMBL:CCG47251.1};
GN OrderedLocusNames=HBHAL_4914 {ECO:0000313|EMBL:CCG47251.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG47251.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG47251.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
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; HE717023; CCG47251.1; -; Genomic_DNA.
DR RefSeq; WP_014645135.1; NC_017668.1.
DR AlphaFoldDB; I0JSX9; -.
DR STRING; 866895.HBHAL_4914; -.
DR KEGG; hhd:HBHAL_4914; -.
DR PATRIC; fig|866895.3.peg.3952; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCG47251.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 196..286
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 395 AA; 43792 MW; DC7065D0D6A13F7F CRC64;
MRTKNADLVR RSQELHSSLV KWRRDFHQHP ELSFQEQRTS RKVEEILREA GIEDIETNVG
GYGLIATISN GPGAVIGVRA DMDALPIEEE TGFAWASKNH GVMHACGHDA HTAILLGVAH
LFIEDAKANR FQGTVKFVFQ PAEEKCDEQG ETGAVKMLHS NKLEELDSIL ALHMCPWRKR
GEVQIHDGPS MANNDEFHIA IKGDGGHAGY PHQTVDPVWI STFVLQNLYS LNGRKVDPLD
VGTISIGKIR AGEANNIIPH EVEIRGTMRS YSNEVRYMLI HEINKIPSLV ASLGGECDLV
VQKGEPALYN APEINAVFRK AAYPMTIYNE PFGMGSEDFS HFTQKIPGAM FFLGCATEKV
TNLHQSDFNI DESAMCDGVR VLAESTYELL KQGGI
//
