ID A0A179D2I9_9BACT Unreviewed; 768 AA.
AC A0A179D2I9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Type II secretory pathway, ATPase PulE {ECO:0000313|EMBL:OAQ20193.1};
GN ORFNames=TDIS_1695 {ECO:0000313|EMBL:OAQ20193.1};
OS Thermosulfurimonas dismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ20193.1, ECO:0000313|Proteomes:UP000078390};
RN [1] {ECO:0000313|EMBL:OAQ20193.1, ECO:0000313|Proteomes:UP000078390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S95 {ECO:0000313|EMBL:OAQ20193.1,
RC ECO:0000313|Proteomes:UP000078390};
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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:OAQ20193.1}.
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DR EMBL; LWLG01000014; OAQ20193.1; -; Genomic_DNA.
DR RefSeq; WP_068671282.1; NZ_LWLG01000014.1.
DR AlphaFoldDB; A0A179D2I9; -.
DR STRING; 999894.TDIS_1695; -.
DR PATRIC; fig|999894.6.peg.1692; -.
DR OrthoDB; 9805147at2; -.
DR Proteomes; UP000078390; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 509..644
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 25..52
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 768 AA; 87844 MW; 8740B5DB75F60A68 CRC64;
MDTDIKAYIE NKLKEAELYA KQGLVDEALE LYRELKNLVS EEQDELKKEI QKRIFELEAF
KGIVSEEVLE ETPQEERLKK ALILKDGAFY QQAIKILEEL LEEGFKTLEV YKNLAECLGN
IGQFERAAHI IRQALKEIPA TAENKLDILN LKKLLAEYLE KAYEFDEALR LYIQLANEVE
EKDTIQEKIE YLKNITTNCR RLKFLLKERI ITPSICQEAA EIAKETNSSI ESVLIEKFHI
SKDKIGEALS RFYNCPFIEI SDDKIVIKPK CLEGVKENFL RQTLIAPLEE EGKIFLLTED
PFNLDQIEQA KKILNLKEFE VAVGIREDIL KLIDLYYGKL TFQPPEAPEL ELIEEEEAHE
EEEPLPEDQE SVVVQLANYI LEEAYNRGAS DIHIESLTGR RGAQIRFRID GECIPFQMVP
YSLKRPLISR YKIMAGLDIA EKRLPQDGKI KFRTRTGKVF EVRVATLPTI ENNEDVVMRI
LGGVQARTLE EIGLRPEVME QFKKLLEMPY GLILVVGPTG SGKTTTLHAA LHYINRPNKK
IWTAEDPVEI VQEGLRQVQV KPKIGLTFAR VLRAFLRADP DIIMIGETRD EETAHTLIEA
SLTGHLVFST LHTNSAPETV TRLLGMGIDP YNFADALLGV LAQRLAKRLC PDCKKPYHPT
DKEIEELIFE YGEHPLKPLT EEEVKQATLY RSVGCSRCNH TGYRGRIAIH ELLIPNDELR
ELIVKAAPVH EIREAAMRNG MYTLKQDGIF KVLAGDTDLK QIRAVCVR
//
