ID A0A2L2XNS3_9FIRM Unreviewed; 1298 AA.
AC A0A2L2XNS3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Flagellar hook-length control protein FliK {ECO:0000313|EMBL:GBF35621.1};
GN ORFNames=DCCM_4750 {ECO:0000313|EMBL:GBF35621.1};
OS Desulfocucumis palustris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfocucumaceae;
OC Desulfocucumis.
OX NCBI_TaxID=1898651 {ECO:0000313|EMBL:GBF35621.1, ECO:0000313|Proteomes:UP000239549};
RN [1] {ECO:0000313|Proteomes:UP000239549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAW-5 {ECO:0000313|Proteomes:UP000239549};
RA Watanabe M., Kojima H., Fukui M.;
RT "Genome sequence of Desulfocucumis palustris strain NAW-5.";
RL Submitted (FEB-2018) 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:GBF35621.1}.
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DR EMBL; BFAV01000179; GBF35621.1; -; Genomic_DNA.
DR Proteomes; UP000239549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR017313; Moth2364.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
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; PF04151; PPC; 1.
DR Pfam; PF00395; SLH; 2.
DR PIRSF; PIRSF037899; Subtilisin_rel_Moth_2364; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51272; SLH; 2.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000313|EMBL:GBF35621.1};
KW Cilium {ECO:0000313|EMBL:GBF35621.1};
KW Flagellum {ECO:0000313|EMBL:GBF35621.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000239549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1143..1206
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1240..1298
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 37..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1298 AA; 136361 MW; E4057AF89ED9934C CRC64;
MMFLHNRAGK KWALAMAALL ILAGLKFYIV DTGNSGTPPA HRAGGENRSN AEKAEKAGEA
PQSGGDSGFV EINVSVKDEK EKLIIKQMVD SSGGEVIKGF DEKGTTLRVK VSEQMADQLK
ANSSVINTET FVQPEFLNDR SSGIIGARTV QTPGYVLPGG LKGAGQVVAV ADSGLDTGDD
KSGIHPDFMF EKGKEPKIVA LKSLSGNLLP SDPIGHGTHV AGTVLGTGAA SDGKYRGVAP
EARLYFQSIL NVKDQADPPA NLNELFAPAY AAGARIHVNS WGTPVNQYTA ASSQIDDFTR
KHPDFLALFG SGNGGPGHGG QGTVVAEANS KNALSVGASE NPRPGFGSDS DDVADIASFS
SRGPAADGRI KPELVAPGTE IISTRSSLAP TNFLLNHFYT RMDGTSSSAA LAAGAATLLR
EYFKSVGPDS SPSSALLKAV LINGARSIGN GTRAEGFGML DVQGTVLSLQ GRSVICRDDR
KGLEENKTAQ YSYNVTDSTR PLKITLSWCD PPQAPGASGK TLVNDLDLTV TGPDGRVFYG
NDFGGQGKRD SVNNTEQVRI DRPRPGKYVV EVRGAAVGVD AVTSSPGVNQ DFAVAFGQPP
ARGIIASINK SGQIKLAGGG VLTPLPGADI HLSRDGIEPE GDPAGFRLAA GSDIYYFPSE
NGVKDIYVSY VTAFSGSVKG AESDGRKMLL ELRPEYSEGG YNISPSPEVT INVNGSRAKL
INEILPGSDV VGVINPLTGY MWSADATYQV VTGKVAGPGA EAGEITLESG ETYRLSRQAG
INVENKWEAY GPEDEAFSFS SLKKLECVKP GSKVLMVISP RTREVGTLNA ENKMISGRVA
RITRFGVATL ESGLQFKLPD SALVFKNGGQ SSPGAVKSGD WIEGVCSDSG ITENGLNVVE
RLWAYSGVVY GMAGNILPDP GIILLKREEG KTDSYRTAKN AACFVEGLPS GLDAVESGYY
LRALLNGNGE VIRLDAVEPV NEEITISLLA EDNGSTTIRT ADGKSYVLER DAEIYKEGVM
VAPGDLAPGE KAKITLLPDS SDGLDKVIMV ESRPGPGVNP PPLEFILEPD SGEGKTLLRG
KTAGNMVYYC IDGGSWNSAA VTGGVFAAGL DLPVPGKHKI VLGSVNRATG GINVMTRDFY
GFEAGYPKDG FQGHWAENYI TAVLGAGLMK PDSGGKFSPS APVAAGDFYE ALYALTGVPV
EEFEVRGGTG AAVTRLDAVT ALWRAAAARG IGRNYSASAP PPFGDWDDIP GSRRDEVAWC
YNSGIVAGTS AGKLEPGRYL TRAEAAVMIW RLSGLIYE
//
