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Database: UniProt
Entry: C0QHZ8_DESAH
LinkDB: C0QHZ8_DESAH
Original site: C0QHZ8_DESAH 
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
//
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