ID S3NAT9_9GAMM Unreviewed; 578 AA.
AC S3NAT9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=General secretion pathway protein E {ECO:0000313|EMBL:EPF71484.1};
GN ORFNames=F945_02513 {ECO:0000313|EMBL:EPF71484.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71484.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF71484.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71484.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) 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:EPF71484.1}.
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DR EMBL; ATGI01000032; EPF71484.1; -; Genomic_DNA.
DR RefSeq; WP_016656913.1; NZ_KE340353.1.
DR AlphaFoldDB; S3NAT9; -.
DR STRING; 632955.GCA_000829675_01728; -.
DR PATRIC; fig|421052.3.peg.2457; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_6_6; -.
DR OrthoDB; 9804785at2; -.
DR Proteomes; UP000014568; 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 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 PANTHER; PTHR30258:SF13; SECRETION PATHWAY ATPASE-RELATED; 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:UP000014568}.
FT DOMAIN 395..409
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 578 AA; 66165 MW; A0D95E997A4AF641 CRC64;
MHVDFNIDST WCLQQLHQDG LITQRDLDLV RTTPRRTEQQ SWHALQWIAH FKLCNLEHKS
TLNLNDLCLW LAKKSGLALY TLDPLKLDIA ALTQIMSQEF ALKNHILAVE IQQDQVWIAT
TQPFNQQWIP QLAMSLKPKN ISVVLLDPET MQRYQSEFYS INQATYAAKK QYDRHQFAEP
AIIQVESELD EQHIVQLVDW LLQFAFEQRA SDIHLEPRQI QGQVRFRIDG LLHCVHRMPM
TTFNAVVARL KILAQLNVAE RRRPQDGRLA MQTSHKEQRE LRISTLPTAF GEKMVLRIFD
PMLLLRDLSQ LGFSANLLAT WQQLIQARNG MILVTGPTGS GKTTTLYSTL KQCATEQFNV
CSIEDPIEML EPSFNQMQIN PKIDLGFAEA IRALMRQDPD IIMVGEIRDQ RTAQMAIQAA
LTGHLVFSTL HTQDAVSSLI RLQDLGIQPF LIAATLLGIL AQRLVRRLCP YCKQLALVDA
IKWQHLVADY HYVQPEQLYR ARGCPHCRET GFVGRIALYE FLPITTALKQ QIIQGNQHLH
IREAVYKAGI LPLRIAAAEQ ILQGETSLDE VFTVLPWG
//
