ID D5H8J9_SALRM Unreviewed; 578 AA.
AC D5H8J9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Peptidase M16 inactive domain family {ECO:0000313|EMBL:CBH24354.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:CBH24354.1};
GN OrderedLocusNames=SRM_01433 {ECO:0000313|EMBL:CBH24354.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH24354.1, ECO:0000313|Proteomes:UP000000933};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M8;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-95(2010).
RN [2] {ECO:0000313|EMBL:CBH24354.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH24354.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [3] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FP565814; CBH24354.1; -; Genomic_DNA.
DR AlphaFoldDB; D5H8J9; -.
DR KEGG; srm:SRM_01433; -.
DR HOGENOM; CLU_009902_1_2_10; -.
DR Proteomes; UP000000933; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:CBH24354.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..172
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 218..315
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 322..498
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 163..218
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 578 AA; 64630 MW; 53753B316E4CBC22 CRC64;
MMAVSTRGGI GSFYGAGCGE NVKLSIKGGA GRGETVSNQR SRSVIKHAPR HSHFKESLCL
MNWTSLREGW SRVGLTLTAL LVLLAGAALP AQGQDLLRQF EDKVTTFTLD NGLDFVVVER
HDAPVASFAT YADVGSVDEP QGKTGIAHMF EHMAFKGTTT TGTKNIEKEM QALERQEEIY
LQLRRERAKG PQADSSRIAE LEEQFEQATT EAESYIEKGE FENILERNGV SGLNATTSAD
ATRYFYSLPA NKAELFFALE SDRFANPVLR EFYTERDVVM EERRQRTESS PTGRLVEEFL
TTAFKAHPYG NPTIGHMSDL KKLSRTDAKQ FFEKHYSPRN LTIGIAGDVD PEQMRAFAEK
YFGDLPGGDE PLPVRTEEPE QISERRVVIR EQTQPFVMIG FHRGSMQSED APVYDVLSDV
LTGGRTSRLY ESLVTEEKAL QVQALPAFPG SKYDTMFGIF GVPNRGVSPD SVEHMIYDEL
EAIKEDGISQ EELERAKTRA RSDLIGQLDS NQGLALQFAQ MEELKGDWRS VFRRLDAIQA
ITVEDVQRVA QNTFRRSNRT VAMIKTTDDE QQPTTAAN
//
