ID C0QHZ8_DESAH Unreviewed; 684 AA.
AC C0QHZ8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Alkaline serine protease (Subtilase family protein) {ECO:0000313|EMBL:ACN15734.1};
GN OrderedLocusNames=HRM2_26400 {ECO:0000313|EMBL:ACN15734.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15734.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN15734.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP001087; ACN15734.1; -; Genomic_DNA.
DR RefSeq; WP_015904497.1; NC_012108.1.
DR AlphaFoldDB; C0QHZ8; -.
DR STRING; 177437.HRM2_26400; -.
DR KEGG; dat:HRM2_26400; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_9_0_7; -.
DR OrthoDB; 9765693at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR017315; Pep_S8A_subtilisin_pbac-2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF17957; Big_7; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037901; Subtilisin_rel_Nmul_A1891; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 141..382
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 684 AA; 71769 MW; E06EA7651FD40F1F CRC64;
MIKRLKTNLQ TIVTIAIAMV LVLAGSGLVQ ADSKKFVPGE LLIQVKQGVT KGAVDKLLNS
YDAATAGEIE SIKTRRIKVP VHALEQVKKA LSKNPNIQFV EENFYAEAGY VPNDDRYSSQ
WHLPMISAPG AWDLTTGSPS VPIAIIDSGV DPTHPDLAGN LIAGYNFLEN NTDTQDVLGH
GTAVAGSAAA MTDNITGVAG VAGDSPIMPL VVLDANDYAT YYDIARAINY AADQGVRIIN
ISIGGSSYSS TLQNAVNYAW NKGAVIFACA HNYSTDTPYY PAACANVVAV SATTSTDTFA
SFSNHGDWID ISAPGTYILT TSRGGGYGNW NGTSFSSPIT AGVAALILSA NPSLTNTQVV
NILTQSADDL GSTGFDNYFG YGRVNALQSI LAALAAVPEE DTIDPSVAIT SPQNDTTVNG
SLTVSVSATD EGGVDRVELH VNGELLSSDT TSPYTFSWDT YGYANSDHEL MAVAYDTAGN
AGWSSVITVT VANESDDDTQ APVVAITSIQ GGALVSGGIT VDVSATDEGG VALVELYLDG
VLLDEHITSP YAFFWDTTAY ANGTYALVAV AFDTAGNQGV SEAINVSVDN VIFEDTEAPV
VTITSPGDGA SIGNRETVQA SASDAGGISR MELFLNEELT AVKYKSELSW NWNTRKLSKG
TYTLSVKAFD TAGNEGIDTI TVYK
//