ID A3U7P7_CROAH Unreviewed; 956 AA.
AC A3U7P7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:EAP88264.1};
GN OrderedLocusNames=CA2559_05875 {ECO:0000313|EMBL:EAP88264.1};
OS Croceibacter atlanticus (strain ATCC BAA-628 / HTCC2559 / KCTC 12090).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Croceibacter.
OX NCBI_TaxID=216432 {ECO:0000313|EMBL:EAP88264.1, ECO:0000313|Proteomes:UP000002297};
RN [1] {ECO:0000313|EMBL:EAP88264.1, ECO:0000313|Proteomes:UP000002297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-628 / HTCC2559 / KCTC 12090
RC {ECO:0000313|Proteomes:UP000002297};
RX PubMed=20639333; DOI=10.1128/JB.00733-10;
RA Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT "The complete genome sequence of Croceibacter atlanticus HTCC2559T.";
RL J. Bacteriol. 192:4796-4797(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP002046; EAP88264.1; -; Genomic_DNA.
DR AlphaFoldDB; A3U7P7; -.
DR STRING; 216432.CA2559_05875; -.
DR KEGG; cat:CA2559_05875; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_328936_0_0_10; -.
DR Proteomes; UP000002297; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00306; Peptidases_S8_S53; 1.
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; 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; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 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:UP000002297};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 158..424
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 389
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 956 AA; 104651 MW; F17F8C0B20E566CB CRC64;
MLSLSTTLLS QEYKSFYLEL ASGIGVDLLD GSQIVIQPDQ TIKLVTNQTH PIFDFLNSKP
FYSIEKAFPM TSLPRLKKVY IISIKDDTLV TDFVNNTGIT YFKEIDDDNN ILTSTTTAVN
NTQISIPNDY EDLLYGGNNA SLELINAPLA WAITTGDSNI LVGVVDSSYE LNHPDLTGQI
VNNIEVVPSN FSHGTAVASI IAANTDNNEG LSSLGRDLKL VTATCGGGGN NLVSGLEELA
DYPGVRVINC SWRICEGSPV KTYLDDVMDY VRTKDILVVA SAGNGVQGDG TVKGCDSDGN
GYGYPGSYDD AISVTGVGHR FSIGTLQDNI PGQTKSWIDV HRQLPDNPNN FASHTHNDKV
NVSAPGIYVL SATETSNNQT GYTAGIGTSS STPLASALAG LIFSINPNFT ATQVKDIIES
TTDNIYDIDL NQPYIGELGT GRINAYAAVL KAQCLTNPES GLDLAMQNSQ LDNFEEPDTL
TTQPYRSKDI WVRNQDDGLL VKEHQNPEYD SNNPNYVYVR VTNSSCDSST GSDPLKLYWA
KANTALSWPD HWDGSLTMTD PITGEDILMG DQIGTVNIPP LDIGQEAILT FEWLVPNPED
YENINPNPWH FCLLARIDTP NDPMTTPEND NIVLNVWNNN NIVWKNTTVV DVVENSSNYG
GVVAVGNYSN QQQSFDLVFV KDANEKGKAI YEEAEVGLEM DTTLYNAWQD GGKSQSQLKS
TKDDYKKILT TNNSKLGNII LDAGEIGTLY VSFNFFTNQS TSKDKFALSV LQQDATTGSL
IGGEEYIINK KTSSSFRANA GEDQDIKKDE FIVLSATPIN EDVTFNWYDQ NNTLLYSGEN
VLVNPEFTST YKLEVISNLN GFKDYDHVDI TVNPFYLESL IPNPANNLVT VQYKVDEASS
AYLSVVNTAT GQHHNYILDT TQTSRLLDIS NLSSGIYSII LVCDGEIQDS LNLSKL
//