ID G9YCX4_HAFAL Unreviewed; 240 AA.
AC G9YCX4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=LPS-assembly lipoprotein LptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN Name=lptE {ECO:0000256|HAMAP-Rule:MF_01186};
GN ORFNames=HMPREF0454_04452 {ECO:0000313|EMBL:EHM38332.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM38332.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM38332.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM38332.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with LptD, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane. Required
CC for the proper assembly of LptD. Binds LPS and may serve as the LPS
CC recognition site at the outer membrane. {ECO:0000256|HAMAP-
CC Rule:MF_01186}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptD. {ECO:0000256|HAMAP-Rule:MF_01186}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_01186}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_01186}.
CC -!- SIMILARITY: Belongs to the LptE lipoprotein family. {ECO:0000256|HAMAP-
CC Rule:MF_01186}.
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:EHM38332.1}.
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DR EMBL; AGCI01000105; EHM38332.1; -; Genomic_DNA.
DR AlphaFoldDB; G9YCX4; -.
DR PATRIC; fig|1002364.3.peg.4005; -.
DR HOGENOM; CLU_103309_1_0_6; -.
DR Proteomes; UP000005959; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR HAMAP; MF_01186; LPS_assembly_LptE; 1.
DR InterPro; IPR007485; LPS_assembly_LptE.
DR PANTHER; PTHR38098; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR PANTHER; PTHR38098:SF1; LPS-ASSEMBLY LIPOPROTEIN LPTE; 1.
DR Pfam; PF04390; LptE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01186};
KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_01186, ECO:0000313|EMBL:EHM38332.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01186};
KW Palmitate {ECO:0000256|HAMAP-Rule:MF_01186};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01186}.
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 240 AA; 25796 MW; 43B94C0B6B5586EF CRC64;
MTSLLKIAVL GLAVLTAGCG FHLRGNTSVP TEFQKITFDT SDPYGPLSRS IREQLRLSGI
TIVDPKADDS SKDPVSTNST SIVDNSAAAA KPADGSDKLP SLRIVGSSES KETVSIFKDG
KTAEYQMVLN VSAQVLVRGH DLYPLTVRVY RSFFDNPLTA LAKDSEQEMI RQEMRDQAAQ
QLVRKLLSVH AAELQNNDNR MNAEVTAPKV QSANDFNSVS TDTTSTPAST TTATGSISAQ
//
