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Database: UniProt
Entry: K4LJ07_THEPS
LinkDB: K4LJ07_THEPS
Original site: K4LJ07_THEPS 
ID   K4LJ07_THEPS            Unreviewed;      1376 AA.
AC   K4LJ07;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Serine protease/ABC transporter B family protein TagC {ECO:0000313|EMBL:AFV12981.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:AFV12981.1};
GN   Name=tagC {ECO:0000313|EMBL:AFV12981.1};
GN   OrderedLocusNames=Tph_c28160 {ECO:0000313|EMBL:AFV12981.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV12981.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV12981.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 26808 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R., Gottschalk G.,
RA   Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of the
RT   fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; CP003732; AFV12981.1; -; Genomic_DNA.
DR   RefSeq; WP_015051840.1; NZ_KI912609.1.
DR   STRING; 1089553.Tph_c28160; -.
DR   KEGG; tpz:Tph_c28160; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_269152_0_0_9; -.
DR   OrthoDB; 900053at2; -.
DR   Proteomes; UP000000467; Chromosome.
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; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR001119; SLH_dom.
DR   InterPro; IPR034058; TagA/B/C/D_pept_dom.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF00395; SLH; 3.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51272; SLH; 3.
DR   PROSITE; PS51892; SUBTILASE; 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:UP000000467};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          1192..1255
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1256..1316
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1319..1376
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        275
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        461
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1376 AA;  145758 MW;  BA08436144E4A9F2 CRC64;
     MRRLVVCCAA IVLACFLVVE AIPVFSRQVD THPQETSGAE EGERMVPPEN PVGLFLMPVR
     EGEEVPRETL AALGLEKGDP LGRETLLVRL PLNKVEEAKE KGVFLRPYSA ADRLAPGLQG
     KKGSEQEIEV LVTLFRSSDR EGFVRKVPEL GGEVLAGLEG EGRVLRLRLP EGALAELAAS
     PEVVYVEPAQ EYRFYNERAR DLVGAAFLQA AGFLSPEWMG LSGRGQIIGL ADSGIDAGSP
     GDIHPDLQSL PGQMPKVVML KSWAGAATAA DFNGHGTHMA ATVAGTGAAS QGRFKGIAPG
     ASIYFQGLLD ESGKLTPPPD LTVLFEPAYA AGVRVHINGW GGEKGGYFGT ASQIDRFLRR
     CPDFLAVFSA GNGGPQAGKL TPEAYSKNAL VVGASQSPHP LFNPAQNDAG SISSFSSRGP
     TADGRIKPEL YAPGSLISAR SRLADLPSAL SDGYTYLEGT SMAAAVAGGG AALLREFFQR
     IEKLAAPSAA LVKAALICGA RTPQGWPNSS GFGILDLGGT VLSLWEKNFR YVDAEEGVAA
     GETLSYTFEV KSGESPFKAT LVWTDPGAAP GAEAPLVNNL DLVVRGPEGS EWIGNSFLSD
     RPDDVNNVEQ VVIPAPKPGI YTVYVKGKAI TKGVTHRDGR PAQDFALVYG QPLVRDVVTA
     AGAQGPVLES GRVLAAAPQQ VRFALNGEVA SWPVSDNGGS LGKVLPGADV YFPPGYASRG
     SIYIVGRTFR AVGVQVLDAG GRYLLTEINP EARSGGLYFA PAAEKGVLIN GVPAAGPASV
     PPGGGVTAWI NPGSWEIWGA EFSFSAVEGL LGGVDMAKRE LTLIGVEKTY SLAPQAALAY
     SDEMVDVDAA DLPFGAAATP CWENLLPGLR VRLVLSPATG EVTYVAARRE LAVGMIAEVD
     VMNRRIVLST GRDYTVPVGV SLSLDEKEAH LQDLRPGQYA VGVLLPKTRQ VLSLSAYSSF
     LYGQVVYTSL RDGTIYFVDN CGRSGAYRYQ EDTGFYRWGL PAVAAAAEAG CWARLILKPG
     ENLIWRLDVA ETTAERREIV AGYDEETGTL ITSQGRYRLT ERTSITKNGY PVAAWDLVPG
     EEVALTPFLE GASGEPMLAA VAARTSAGTR APELEVTASW RQGEVVLMGS TTADRLYLYP
     EKGDRMSIPV DGKGSFHLSF RPEKEGENFL LVVAVDGGSG GVTGRQLTVS PGTGAVFRDV
     AGHWAERAIE ELAARGVLKG YPDGTFRPDD PITRSEFTVL VTTALGLSGG EAELPFADAG
     SIPSWARPAV ERAYLHGLVR GSADGCFRPA RKITRAEAAA VLSGALSVIN FREDTPVSPP
     HWRDDGAIPT WARPAVERVY AAGVMTGRPN GFFAPGEILT RAEAVSAVRR LLERTP
//
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