ID D2PYN6_KRIFD Unreviewed; 429 AA.
AC D2PYN6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADB29882.1};
GN OrderedLocusNames=Kfla_0763 {ECO:0000313|EMBL:ADB29882.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB29882.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB29882.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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; CP001736; ADB29882.1; -; Genomic_DNA.
DR RefSeq; WP_012918438.1; NC_013729.1.
DR AlphaFoldDB; D2PYN6; -.
DR STRING; 479435.Kfla_0763; -.
DR KEGG; kfl:Kfla_0763; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_13_3_11; -.
DR OrthoDB; 614750at2; -.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR023834; T7SS_pept_S8A_mycosin.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR03921; T7SS_mycosin; 1.
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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000007967};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003033422"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..326
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 429 AA; 44705 MW; 1A664FD6BEE02350 CRC64;
MSARRFVCTL AAGALAAGWP AIAAAPAAAA PPRGACTNPE PGRSTESLLP WAQQLLKPQR
AWPFSTGSGV TVAVVDSGVD ADHPQLRRPG KVLRGRDFHL VGSLPGNYDC VSHGTGVAGI
IAAGPATGIG FAGVAPGARI LPVRISERDS ADNGRTELID PVILAKGIRY AVDQGARVIN
LSMSGDRDQA PVRQAVEYAV KRDVVVVAAV GNRQQTDGER LPSFPAAYPG VLGVGAIDNA
GARLSGSQTG PYVDLVAPGG SVLATVRQHG HAYVDGTSYA APFVSGAAAL VRAAWPKLTA
RQVVQRLTAT ASPARGGSDS TQYGAGIIDP YRAVTEGMVG TRMRQVPPMT VPPPDQQRLA
AAAWWRSAGV DAQRLTALAV AGALTALLAG WLVVAGRRRR WFAGRTTIGH QQRPDLAELP
PEYLFTRQD
//
