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Database: UniProt
Entry: B7GKY1_ANOFW
LinkDB: B7GKY1_ANOFW
Original site: B7GKY1_ANOFW 
ID   B7GKY1_ANOFW            Unreviewed;       744 AA.
AC   B7GKY1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Subtilisin-type proteinase with two SLH domains {ECO:0000313|EMBL:ACJ34959.1};
GN   OrderedLocusNames=Aflv_2606 {ECO:0000313|EMBL:ACJ34959.1};
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34959.1, ECO:0000313|Proteomes:UP000000742};
RN   [1] {ECO:0000313|EMBL:ACJ34959.1, ECO:0000313|Proteomes:UP000000742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CP000922; ACJ34959.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7GKY1; -.
DR   STRING; 491915.Aflv_2606; -.
DR   KEGG; afl:Aflv_2606; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_373269_0_0_9; -.
DR   Proteomes; UP000000742; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
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   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF00395; SLH; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51272; SLH; 2.
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:UP000000742};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..744
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002855989"
FT   DOMAIN          561..624
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          682..743
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        256
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        412
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   744 AA;  82623 MW;  AF6682ADE31E7A7B CRC64;
     MASVSRWLWL CVVCFLFPSV VQADEKEEWI VQVQHPSNFS DIQSYVVDTV GTFAKVVVTE
     EEREHISRLP FVLKMEKNDM KRAAVNDPLF SEQWSLGMVR WHFPTVTSVN RLIGKTMIVD
     GREEVYDGEA FFGEHIVIAL GEETLSRLSV TVDHIEGPWR IQVKDEKGAT LGENEGELPR
     LDVLIPRPSS TIHLYVTAPN WTNRPRIVEL KGVNHVLVAV VDSGVVQHED LNDHVLYSVS
     VDYAENKRYA DDTFGHGTHV TGILAASVNN GKGIAGLIGD APVDILPIKV LDRYGVGGDF
     EIAKGVKYAL EQGASIINLS LAGQGETEVL KAVIEEAVKR GVHVVAAAGN SHMPTTNIYP
     ASYPGVITVA AVDRQQMPLS ISNYGWDVEV SAPGDFLIST YPSGYRAMRG TSMAAPHVSA
     LLAVLRAMYP EEDAFQLRSR IWKTAKDVYW RGYDMYTGYG IIQWQQALAL SAPSNIDWLN
     LQPGQPIEKN RTYMLGLSSR FVGKNGHLFI NGKLVHSFVI HQEMMPFRLF DLAKQQGDVA
     VVITDEQQRV IASDVRAVPI RPTPFSDVKK TYWAYSDILQ AQQFGMIRGY GDGTFRPNTP
     LTRGESMVML ARLFGWEVPS LLSAPFVDVP LTATNALLVA TAAEKGIVKG TEGKALLHEQ
     LTRGQFALLL MRALQLENEP IRSVSPFQDV TQQDMWKAVQ LLAERGIVAK TSYFHPNEPV
     TRAQMCAMLV RVSTLIRQYS TKTA
//
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