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Hemolysin secretion ATP-binding protein HlyB (HlyB protein) (Type I secretion system permease/ATPase)

 Q1M2T2_ECOLX            Unreviewed;       707 AA.
Q1M2T2;
30-MAY-2006, integrated into UniProtKB/TrEMBL.
30-MAY-2006, sequence version 1.
25-APR-2018, entry version 86.
SubName: Full=Hemolysin secretion ATP-binding protein HlyB {ECO:0000313|EMBL:CAM84370.1};
SubName: Full=HlyB protein {ECO:0000313|EMBL:CAK02716.1};
SubName: Full=Type I secretion system permease/ATPase {ECO:0000313|EMBL:PIM26263.1};
Name=hlyB {ECO:0000313|EMBL:CAK02716.1};
ORFNames=AL530_025365 {ECO:0000313|EMBL:PNP66171.1},
CT143_24035 {ECO:0000313|EMBL:PIM26263.1};
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562 {ECO:0000313|EMBL:CAK02716.1};
[1] {ECO:0000313|EMBL:CAK02716.1}
NUCLEOTIDE SEQUENCE.
PubMed=17064280; DOI=10.1111/j.1574-695X.2006.00140.x;
Sheshko V., Hejnova J., Rehakova Z., Sinkora J., Faldyna M., Alexa P.,
Felsberg J., Nemcova R., Bomba A., Sebo P.;
"HlyA knock out yields a safer Escherichia coli A0 34/86 variant with
unaffected colonization capacity in piglets.";
FEMS Immunol. Med. Microbiol. 48:257-266(2006).
[2] {ECO:0000313|EMBL:CAM84370.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ABU 27 {ECO:0000313|EMBL:CAM84374.1},
ABU 37 {ECO:0000313|EMBL:CAM84378.1}, and
ABU 83972 {ECO:0000313|EMBL:CAM84370.1};
PubMed=18039831; DOI=10.1128/IAI.01215-07;
Zdziarski J., Svanborg C., Wullt B., Hacker J., Dobrindt U.;
"Molecular basis of commensalism in the urinary tract: low virulence
or virulence attenuation?";
Infect. Immun. 76:695-703(2008).
[3] {ECO:0000313|EMBL:PIM26263.1, ECO:0000313|Proteomes:UP000231393}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ABU 84 {ECO:0000313|EMBL:PIM26263.1,
ECO:0000313|Proteomes:UP000231393};
Stork C., Kovacs B., Trost E., Kovacs T., Schneider G., Rozsai B.,
Kerenyi M., Emody L., Dobrindt U.;
"Whole-genome draft sequences of nine asymptomatic Escherichia coli
bacteriuria isolates from diabetic patients.";
Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:PNP66171.1, ECO:0000313|Proteomes:UP000053643}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FDAARGOS_170 {ECO:0000313|EMBL:PNP66171.1,
ECO:0000313|Proteomes:UP000053643};
Goldberg B., Campos J., Tallon L., Sadzewicz L., Sengamalay N.,
Ott S., Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S.,
Geyer C., Sichtig H.;
"FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
Supporting development and validation of Infectious Disease Dx
tests.";
Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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EMBL; AM261284; CAK02716.1; -; Genomic_DNA.
EMBL; AM690759; CAM84370.1; -; Genomic_DNA.
EMBL; AM690760; CAM84374.1; -; Genomic_DNA.
EMBL; AM690761; CAM84378.1; -; Genomic_DNA.
EMBL; PENR01000021; PIM26263.1; -; Genomic_DNA.
EMBL; LORS02000001; PNP66171.1; -; Genomic_DNA.
RefSeq; WP_000376541.1; NZ_PIJJ01000009.1.
PATRIC; fig|562.10500.peg.127; -.
eggNOG; ENOG4108JJA; Bacteria.
eggNOG; COG2274; LUCA.
Proteomes; UP000053643; Unassembled WGS sequence.
Proteomes; UP000231393; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0008233; F:peptidase activity; IEA:InterPro.
GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
Gene3D; 1.20.1560.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR010132; ATPase_T1SS_HlyB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005074; Peptidase_C39.
Pfam; PF00664; ABC_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
Pfam; PF03412; Peptidase_C39; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF90123; SSF90123; 1.
TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
PROSITE; PS50929; ABC_TM1F; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PROSITE; PS50990; PEPTIDASE_C39; 1.
4: Predicted;
ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
ECO:0000313|EMBL:CAM84370.1};
Complete proteome {ECO:0000313|Proteomes:UP000053643,
ECO:0000313|Proteomes:UP000231393};
Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
ECO:0000313|EMBL:CAM84370.1}; Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 153 175 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 187 208 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 264 289 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 295 315 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 3 125 Peptidase C39.
{ECO:0000259|PROSITE:PS50990}.
DOMAIN 158 436 ABC transmembrane type-1.
{ECO:0000259|PROSITE:PS50929}.
DOMAIN 468 703 ABC transporter.
{ECO:0000259|PROSITE:PS50893}.
NP_BIND 502 509 ATP. {ECO:0000256|PROSITE-
ProRule:PRU00434}.
SEQUENCE 707 AA; 79527 MW; 20A39EB9E0CB4AFD CRC64;
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA KSLELKVKQV
KKTIDRLNFI PLPALVWRED GRHFILTKVS KEANRYLIFD LEQRNPRVLE QSEFEALYQG
HIILIASRSS VTGKLAKFDF TWFIPAIIKY RKIFIETLVV SVFLQLFALI TPLFFQVVMD
KVLVHRGFST LNVITVALSV VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI
SYFESRRVGD TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP QMTNIWDKQL
AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTESYHGKLA LPEINGDITF RNIRFRYKPD
SPVILDNINL SIKQGEVIGI VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHVIMRNMHK ICKGRTVIII
AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY LYQLQSD


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