ID F3YYC9_DESAF Unreviewed; 586 AA.
AC F3YYC9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN ORFNames=Desaf_1234 {ECO:0000313|EMBL:EGJ49573.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49573.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ49573.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49573.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034006};
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; CP003221; EGJ49573.1; -; Genomic_DNA.
DR RefSeq; WP_014259373.1; NC_016629.1.
DR AlphaFoldDB; F3YYC9; -.
DR STRING; 690850.Desaf_1234; -.
DR KEGG; daf:Desaf_1234; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_6_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; 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; 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; IPR013369; T2SS_GspE.
DR InterPro; IPR007831; T2SS_GspE_N.
DR NCBIfam; TIGR02533; type_II_gspE; 1.
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 PROSITE; PS00662; T2SP_E; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 406..420
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
FT REGION 16..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64286 MW; 18358E263648F5F8 CRC64;
MSVTLREQMG RVRAMLNPAD SSDAKLSGEV GSGQVRLDND APFQTYPPPS LGKPDSGGRE
PSPEELALEL GLRFVPHVEE GWLDLSLVRG LPIAYLKQNL VLPVKGEAGC LLVLVGNPLR
VEVMDELRLI LTDGGADGRA KAEVNFAMAP AEVILEAINQ TFAQADSRAD QIIQDLGVEE
DDDRLLSELE RGGSEDLLDE TSNAPVIKLV NHILAQAVKS RASDIHVEPF KNELLVRFRL
DGVLHNILHL PKRLQAPVAS RIKIMAKLNI AEKRLPQDGR IEVRIGNRQV DLRVSSLPTA
FGERVVMRLL EKNARLLSLE ELGMGPDHHA EMRRLTQLSH GIILVTGPTG SGKTTTLYAA
LSSINSPDKN ILTIEDPIEY QLDGIGQMQV NAKIDLTFAK GLRSMVRQDP DVILVGEIRD
RETAEIAIQA SLTGHLVFST LHTNDAPSAV TRLIDIGIEP FLVSSAVRTI IAQRLVRVLC
PACKREDTPT AKELREMGLC GDAASVVHRA VGCSECMQTG YRGRTSIYEF MRLTESLQDL
VVRNSDANQI RKLALSEGMC TLRQDGIRRV LNGVTTLDEV MRVTLL
//
