ID Q6AQX0_DESPS Unreviewed; 605 AA.
AC Q6AQX0;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN OrderedLocusNames=DP0525 {ECO:0000313|EMBL:CAG35254.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35254.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CR522870; CAG35254.1; -; Genomic_DNA.
DR RefSeq; WP_011187770.1; NC_006138.1.
DR AlphaFoldDB; Q6AQX0; -.
DR STRING; 177439.DP0525; -.
DR KEGG; dps:DP0525; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_030786_0_0_7; -.
DR OrthoDB; 255388at2; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07345; M48A_Ste24p-like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF13414; TPR_11; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000602};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 5..21
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 219..395
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 476..509
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 605 AA; 67942 MW; 93759C49F10AD509 CRC64;
MYNNFIYFLV AIFIFSFSPN IEPTGSSLWP LLALMALVIG YRGICRRLFR RLAGAGVGSY
LQTERRLSII ALVFYGLGFY LFNLKYYFQF FSLAGHLPAL ADIAALCFFL FLLAVMWAEG
SACHARITGG GQGRWRFIVA NIGSSLPIIL PWMIFSLAVD IVQGLPISGA ENIFVGERGE
LYLFALFFVF VLLLLPPLIR RLWRCTPLPA GPLRDHLDRF CARQKFSAQY FIWPLLEGRA
MTAGVVGVIP GLRYILLTPA IIETMDSDEL DAIMAHEIAH VKRGHIFFYI CLILGFSVIV
GWLIEPLLYT VLSLPPVMAL AVSGRVDSEN LASLASGIPL VLLLVLYFRY FFGFFIRNFE
RQADLYTISV MGSASPLIAA FEKISLFTGT KREEPSWHHF GLGQRIDCLA QAEVDASRVK
RHNRILACCL ASYFIGATLL FFLLNSISVE KMELEYKEKY AIATIIHKAA EEPNNVLWQH
LLGDVYLSQK RTEQALAAYE KTVALDPKNA ELLNNLSWLL LTVEGRELRD PERALALAET
AAFLSQQSHI LDTLATAYWA TGRKGLAVQT ERLALRGDPD RADYYRQRIE MFLGQNYLDS
AAGGS
//
