ID Q2S228_SALRD Unreviewed; 393 AA.
AC Q2S228;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE SubName: Full=Peptidase M16 inactive domain family {ECO:0000313|EMBL:ABC44807.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:ABC44807.1};
GN OrderedLocusNames=SRU_1633 {ECO:0000313|EMBL:ABC44807.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44807.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44807.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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DR EMBL; CP000159; ABC44807.1; -; Genomic_DNA.
DR RefSeq; YP_445753.1; NC_007677.1.
DR AlphaFoldDB; Q2S228; -.
DR STRING; 309807.SRU_1633; -.
DR EnsemblBacteria; ABC44807; ABC44807; SRU_1633.
DR KEGG; sru:SRU_1633; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_6_1_10; -.
DR OMA; NIREAKG; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000008674; Chromosome.
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; 2.
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:SF224; PROCESSING PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABC44807.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT DOMAIN 23..111
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 137..314
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 393 AA; 42551 MW; FF66AEA4692445DD CRC64;
MTNPDLAAGD ALRQQLTVSL LDKGTEHRDR FALARVLEAC GAKLDLSSDG LFVEMSGRAL
VDDLPRVLEV AAEMLRAPAF DPEEFRKARA QVAADLQRRM EKTSAQASTA LSQRLFPEGH
PNYSPAPETV LEWLQGLTVQ DVRDYHEAHF GANEWTLAVV GDLQHDAVAS VVDETFAGWA
PHDAPATHDT DAVSTEVGRT TVPMPDKSNV DVRLGHAVPI RRDHDDYPAF YVGNYILGGN
FAARLMSTVR DEMGLTYSIR SSLSGVSTRY VGSWQTSVTL SHDAVDEGIA ATTDVIREFV
AEGATAEELD AKKTTITGSY SVGLATTDRL AQSILTNAER GFDVAYLDDF PEEIRALTLD
EVNAAIQDYL DPASMQEALA GTRPRAAEAT AGA
//