ID D7B229_NOCDD Unreviewed; 419 AA.
AC D7B229;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADH66650.1};
GN OrderedLocusNames=Ndas_1211 {ECO:0000313|EMBL:ADH66650.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH66650.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH66650.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP002040; ADH66650.1; -; Genomic_DNA.
DR RefSeq; WP_013152257.1; NC_014210.1.
DR AlphaFoldDB; D7B229; -.
DR STRING; 446468.Ndas_1211; -.
DR KEGG; nda:Ndas_1211; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_13_3_11; -.
DR OrthoDB; 5240330at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..419
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038440874"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 116..327
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 419 AA; 40921 MW; 84CF645F2C8D2E8E CRC64;
MTAHTDPGTT RSRRRRTAAA ALALGLLAPL PAAPAAAEAP QDPVSLAQVH PFKADNQPCA
ATGGDVVEQR PWTHHFLGLS RAHDLSTGEG VGVALLAPEV DGGVPALADA VEGGQSADCL
GFGTSLAGVV AARSVEDSGL VGVAPDSSVT AVATGSPQTG LASAQEIAAG IGSAVDSGAR
VVLVGTGTWE ASSALESAVA AAEEAGAVVV APATVPTSRG PLPGQPAQHA SVLSVAAHDV
EGLPVAQRPL VLPSGDLARV DLTAPGDRVV GTGPGGGHVA TAGDGVAAAF VAGAAALLMA
REPDLSAAQV RERLTTTAYA SPRGDADPLS GHGRVDPLAA MAIAPGGAPA GVVGEGFVPD
PSPEGSVDAP STAVVVSVGL LLIVLCVLGG AVIKLGRARG WRPAAAGEPV PMRSDEPVR
//
