ID Q21MF4_SACD2 Unreviewed; 573 AA.
AC Q21MF4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Type II secretion system protein E {ECO:0000313|EMBL:ABD80125.1};
GN OrderedLocusNames=Sde_0863 {ECO:0000313|EMBL:ABD80125.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD80125.1, ECO:0000313|Proteomes:UP000001947};
RN [1] {ECO:0000313|EMBL:ABD80125.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024
RC {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; CP000282; ABD80125.1; -; Genomic_DNA.
DR RefSeq; WP_011467346.1; NC_007912.1.
DR AlphaFoldDB; Q21MF4; -.
DR STRING; 203122.Sde_0863; -.
DR KEGG; sde:Sde_0863; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_1_6; -.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0009297; P:pilus assembly; 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; IPR013374; ATPase_typ4_pilus-assembl_PilB.
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 NCBIfam; TIGR02538; type_IV_pilB; 1.
DR PANTHER; PTHR30258:SF1; PROTEIN TRANSPORT PROTEIN HOFB HOMOLOG; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001947}.
FT DOMAIN 389..403
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 573 AA; 62693 MW; 5D53185FE57A0056 CRC64;
MGSQAIVLSG LARRLVRDSV LNEEEARLAL EEATKAKLPL PIYLSQKSGI SALTIATAAS
EEFGTPLCDL RAVRKDSIPV GLVDKKLISK HHALPLFKRG NRLFVALTDP TNLHAIDEIK
FNTGLTTEAV LAEADILNTY IEAYLNAEEE SLSDSLGGLD GDGLDIEAVD EEGRTPGEDT
SEIDETPIVR FVNKVLLDAI KIGASDIHFE PYEKTYRVRY RTDGILKEVA RPPTNLAPRI
SARLKVMSQM DISERRVPQD GRIKMKLSKT RAIDFRVNTL PTLFGEKVVL RILDPSSAKL
GIDALGYEDF QKKLFMDALH QPQGMILVTG PTGSGKTVSL YTGLNILNTP ERNISTAEDP
VEINLEGINQ VNVSNKVGLT FAEALRSFLR QDPDIVMVGE IRDLETAEIG IKAAQTGHLV
LSTLHTNSAA ETLTRLMNMG VPTFNVATTV SLIIAQRLAR RLCSECKIPA DDITNEVLTE
EGFDDIGIDR KDFQLFHPKG CDKCNNGYKG RVGIYEVVRI TPQISRIIMS GGSAIDIADA
AKEAGFFNLR VAALRKAATG LTSLEEANRV TKD
//
