ID A0A0J6FRH8_9BACI Unreviewed; 1409 AA.
AC A0A0J6FRH8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AB986_13640 {ECO:0000313|EMBL:KMM36947.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM36947.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM36947.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM36947.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMM36947.1}.
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DR EMBL; LELK01000004; KMM36947.1; -; Genomic_DNA.
DR RefSeq; WP_048311663.1; NZ_LELK01000004.1.
DR STRING; 157733.AB986_13640; -.
DR PATRIC; fig|157733.3.peg.782; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000035996; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.12090; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
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; PF04122; CW_binding_2; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF04151; PPC; 1.
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:UP000035996};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1409
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039047009"
FT DOMAIN 167..618
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 947..1015
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 370..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 356
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 581
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1409 AA; 151717 MW; FD44B8A5C72B6C80 CRC64;
MKFKKKFLTV VAGTSLIASS FAGVTTYNPE KAEAALTETK KFKLPVTQEI ASLAASEQAK
QELIIVANKH GGPDLTKELE SLGVKVKENT NNYLYLAEVP TRKILQVYRL DSVGMLGANN
EIVLDKNNQE DTDLKPIDKN PGEVVKPATE ETHSATGVDE FHSKYDGTGV KVGIIDTGID
PGHEAFTQYD EDGKIVSTKV KGVLDTVGEG DVWFRQKASE GATITVNEGT YKTEGIDDED
DTYYFGSLEP ASYETDQEGK KLYRDLNGDG KGDSYFDVLL VDDEVYIDTD QDQDFTDEKP
YGEGDIDNLD VDKEDDVAGA NFQIASPSPA YPGTEFPNTT KYPWPVATVF FDGDGHGTHV
SGIAAANGPD LVEEEEEEKE EVKDEEKEEK ATQVNEFGAV AVDGVAPGAD LYGLKVFDSA
GRTYGWSIAN AMYLAAIPEE LGGFGTDVIN MSLGSSPDLN DGSGAYGKII EDMGELYDTV
YVTSAGNAGP GVDSVGAPGD SVKALSIGAY INSKMWATEY GDYPYGKNAD GSPVDGEGLW
YFSSNGPTED GQQKPDFVAP GSAYASFPVH LGNYEVLQGT SMSSPYAAGA VAVLKQAALK
DRIPFDFELA REALIQTAVH IDGYTRVAEG AGLIDVPAAY EYIRKHYINE VKEVNVTVYH
GEKVSGGPGL YVRNKDVPEE VTVMVENPTD ETKNLTISSD SEWFSPSVDN IKLAPGEYKE
MTVSYDKSKM NVGVNAGTLM IDDLDTAYAE ARSFQTIILG EDFKSEDRFR ITHEDEVQAS
KTKSYFFNVK PGAQEIRFAL EALKENDDFQ GRVRMMVINP DGDKVNPFQG YAGYDEEDSP
GIGVEDYVVK SPKTGVWEVA VYGASGPKEG YEMNQYKLEA FVQDVVSSPG KIELGSVIPG
TEVSKSITFE NYLSTKRSVE VVGGAFSKPE TSKTRETVAD KGAYDRTITV KNNISLDVSI
GNTTNGGDDL DLYLYRSKDG KLLGDYIAID ADGDSEESIS LKNLADGEYT IRVDGYSTVD
PTTDFDFSIT EAQVLEPGEK GAGSIEVTGK SSFDLGVGKK ATTDVKITTP EDGGKYTAGI
FLTDKATGEV LSIVPVKTDG EMVDVVAGEN RIETAIEVSK EMYPEGETTD TVFIATGYNF
PDALSAGPLA SAYDAPILLA GSKGTLSDEV LNEISRLKAK NVVILGGENA ISKKVNTQLA
NIGISTADIE RLSGDNRYDT NVQIINKLAE KGSKSEAVFL ATGKNFADAL SAASIAGAND
MPIILTDGKS LTDDAKKLMA GKLVYVLGGD AVISDQVVDM ADEIATTKRL AGANRYGTLV
EIHKELGSTT NNLFVANGRN FPDALAASPL VVKDQGSMFL VESNKIPKEI ESYLVKYFTT
TDVSGATVLG GDNAVNKEVR DQFNKWLNN
//
