ID A0A1E5P1M1_9ACTN Unreviewed; 677 AA.
AC A0A1E5P1M1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=KP-43 peptidase {ECO:0000313|EMBL:OEJ23441.1};
GN ORFNames=AS594_01985 {ECO:0000313|EMBL:OEJ23441.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ23441.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ23441.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ23441.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:OEJ23441.1}.
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DR EMBL; MEHJ01000001; OEJ23441.1; -; Genomic_DNA.
DR RefSeq; WP_069933584.1; NZ_MEHM01000001.1.
DR AlphaFoldDB; A0A1E5P1M1; -.
DR STRING; 285458.BGM19_34840; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000095759; 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 CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399:SF5; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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:UP000095759};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 216..551
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 490
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 677 AA; 72013 MW; 16B829A020FECED3 CRC64;
MARITINGVT VDPLLQSEEL VAASLVSEDA SASNYLLVQT THPPTPEEKE QLSELGVVLQ
EYVPDDTYLC GYRPSDLDAV RALPFVAWAD VYLNGFKIGQ SLRSARLRTG VAELAEPLGG
AGPRPRLVDI VLHEDVDMSE DGLRDRIAAA AGVSYGDVQN DGEKVRITIR DEDLPALASL
DEVKEIEEVP ERVLYNTVSG TLLNAHVSLN GTKFRGEGQI VCVADTGFDK GSTTNVHPAF
TGRVKRLVAL GRTSPERMDD PDGHGTHVAG SVLGDGTSAS MGGPVTGTAP EARLVLQSVM
DENGFLSGIP SNLRKLFEPP FLEDGARIHT NSWGPVTPGL PYNQAAKEAD RMVWDNKDFV
ILFAAGNSGT DQDGDGRINM RSVSGETAAK NVITVGASEG NRPEFSKTYG QLKNGQFRWP
VPPINGDKMA DSPHGMAAFS SRGPSQEGRF KPDVVAPGTS ILSARSRLAP ASQNFGVSTD
PAFMFQGGTS MATPLVAGCV AVLRETLVKN GTPKPSAALI KAMLINGADE LAGQYDPSEA
GPSPNNSSGF GLVNLQRAVV LPTDAGRAGF TDAGELDQGE ERAFHITVPE GGARTLKVTV
VWTDPPGAAL QNDLDLIVRA DGQERHGNMG TGSGFDRVNN VEQVHWQDVP AGEAEVVVRA
HRITLFAQPY AVAWRIL
//
