ID D5UUC7_TSUPD Unreviewed; 428 AA.
AC D5UUC7;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADG77498.1};
GN OrderedLocusNames=Tpau_0863 {ECO:0000313|EMBL:ADG77498.1};
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP
OS 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
OS (Corynebacterium paurometabolum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77498.1, ECO:0000313|Proteomes:UP000001213};
RN [1] {ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
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 Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG77498.1, ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 /
RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RX PubMed=21886861;
RA Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R.,
RA Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Tsukamurella paurometabola type strain (no.
RT 33).";
RL Stand. Genomic Sci. 4:342-351(2011).
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; CP001966; ADG77498.1; -; Genomic_DNA.
DR RefSeq; WP_013125539.1; NC_014158.1.
DR AlphaFoldDB; D5UUC7; -.
DR STRING; 521096.Tpau_0863; -.
DR MEROPS; S08.131; -.
DR KEGG; tpr:Tpau_0863; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_13_1_11; -.
DR Proteomes; UP000001213; 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 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.
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:UP000001213};
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..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039220598"
FT TRANSMEM 405..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..367
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 23..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 320
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 428 AA; 43036 MW; 1BDFD969E614B7D6 CRC64;
MRRALIGAAI AALVIAVGAP STAAAPAVDP PPPDGAPRGP IAPLAPTVQK TQCHTLTTMP
GTDYTRADHA LRTLRYDQAW RFTRGEGQRV AVIDTGVTPH PRLGEVIPGG DYVSSGDGRD
DCDAHGTAVA GIIAARPSAG DSFAGVAPGA SIIAIRQASQ AFEPRDKGVN SHGNMTTMAY
AVTRAVDLGA TVINISEVAC GAFGANLGDD ALARAVKFAY DRNVVVVAAA GNVGTDGACS
AQNEVPGKPV TVASPARFAD VVLTVAATEP DGRAASFSLA GPWVALAAPG TDVTTLEPRG
GGLVNGQTTR QGTSALAGTS FAAPYVAGVA ALVRARYPQL TAAQVRSRIL TTARAAAAIP
AGALGAGIVD PVAALSADLP DGATRTGMID LPPAPPRDDR PRTTALAGAG LLAVAAAAFC
LSRRTRRS
//
