ID B1Y076_LEPCP Unreviewed; 578 AA.
AC B1Y076;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Type II secretion system protein E {ECO:0000313|EMBL:ACB35357.1};
GN OrderedLocusNames=Lcho_3097 {ECO:0000313|EMBL:ACB35357.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35357.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35357.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; CP001013; ACB35357.1; -; Genomic_DNA.
DR RefSeq; WP_012348108.1; NC_010524.1.
DR AlphaFoldDB; B1Y076; -.
DR STRING; 395495.Lcho_3097; -.
DR KEGG; lch:Lcho_3097; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_6_4; -.
DR OrthoDB; 5790493at2; -.
DR Proteomes; UP000001693; Chromosome.
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; 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 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:UP000001693}.
FT DOMAIN 392..406
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 578 AA; 62466 MW; DA189517F2A8A3AA CRC64;
MARPERVRLG DLLVTQGLIS ADQLTQALAA QKTSGRKLGR VFIDNGWVSE IQIAQALAGQ
LRVPFIDLGQ RSVRTEVARL LPEVQARRLR ALVLEETPAG VRVGMADPTD IAAYDEVSRL
VRREIALVVV AESQLLGAID RSYRHTEEIA GLAKELTSEL TSVEVGLGLA GNLGNLGDLL
GMASSSAEDA PVVRLLFSVF EEALRVRASD IHIEPQAGSL RIRFRIDGVL HVQTEADAKI
AAAVALRLKL MSGLDISEKR LPQDGRFAVN LRTGAVDVRI STMPTQHGES VVMRLLNQGT
GLLSIDGMNL PPRVAAALRR AIAKPSGMVL VTGPTGSGKT TTLYAALNAL NNSERKIITV
EDPVEYRLAG LNQVQVHEKI DLSFSRVLRA ALRQDPDVIL VGEMRDQTTA EIGLRAALTG
HLVLSTLHTN DALSTPIRLI DMGVPRYMVA LSLQMVLAQR LLRVICPHCA EPHEPDAHEL
AWLQANGSGA PDLATLRHGR GCNECNHTGY SGRTGVYEFI EMTQELVEAI NHGDPAQFVA
AGRRQMAGHT LARDAAALVL AGRTTVNEAM RISHQLAE
//
