ID A0A2S5TIB8_9GAMM Unreviewed; 764 AA.
AC A0A2S5TIB8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000256|HAMAP-Rule:MF_01411};
GN Name=lptD {ECO:0000256|HAMAP-Rule:MF_01411};
GN ORFNames=C3942_08040 {ECO:0000313|EMBL:PPE74697.1};
OS Solimonas fluminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=2086571 {ECO:0000313|EMBL:PPE74697.1, ECO:0000313|Proteomes:UP000238220};
RN [1] {ECO:0000313|EMBL:PPE74697.1, ECO:0000313|Proteomes:UP000238220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-BB {ECO:0000313|EMBL:PPE74697.1,
RC ECO:0000313|Proteomes:UP000238220};
RA Lee Y., Jeon C.O.;
RT "Genome sequencing of Solimonas sp. HR-BB.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with LptE, is involved in the assembly of
CC lipopolysaccharide (LPS) at the surface of the outer membrane.
CC {ECO:0000256|HAMAP-Rule:MF_01411}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. Interacts with LptE and LptA. {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- SIMILARITY: Belongs to the LptD family. {ECO:0000256|HAMAP-
CC Rule:MF_01411}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01411}.
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:PPE74697.1}.
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DR EMBL; PSNW01000003; PPE74697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5TIB8; -.
DR OrthoDB; 9760225at2; -.
DR Proteomes; UP000238220; 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 GO; GO:0015920; P:lipopolysaccharide transport; IEA:InterPro.
DR GO; GO:0010033; P:response to organic substance; IEA:InterPro.
DR HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR InterPro; IPR020889; LipoPS_assembly_LptD.
DR InterPro; IPR007543; LptD_C.
DR PANTHER; PTHR30189; LPS-ASSEMBLY PROTEIN; 1.
DR PANTHER; PTHR30189:SF1; LPS-ASSEMBLY PROTEIN LPTD; 1.
DR Pfam; PF04453; LptD; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_01411}; Membrane {ECO:0000256|HAMAP-Rule:MF_01411};
KW Reference proteome {ECO:0000313|Proteomes:UP000238220};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT DOMAIN 326..690
FT /note="LptD C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04453"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 86222 MW; 82422508DADD1AD5 CRC64;
MRSRKDRASL HEGPPRDGHG PPSKTILRGQ REPALHPLTR PALHWLALAA GLSLSAPAWA
LEEGNASCPQ LDFGVAAPEP TLDPEQVILN ADHAALEQDG LSKLIGSVRL RQGDKLFSAE
QMDYDDRENT VRVNAESVFR NREMSVRSQE AEFDLDSQTG VFHDSEFTMP SNSARGTAGR
LSLNREGQAE MEKVSFTTCA PDSHGWELHA GDIRMDKATG FGTARNARLD FLGLPILYAP
WFRFPIDDRR HTGLLYPTVG DSDRTGFDMQ VPLYLNLAPN YDATLTPRLM TDRGTQIATD
FRYLLGRGEG KARYEYLSED KKTGEMRDYA HLEHRSLLNA RTSLAMLYDG TSDKTYFEDF
GGRLDLSAIT HLERSARLTY QAPAAYRVQA LVQDFQPLAS SLVAVDDPYR RLPQVLVDAE
TRKSLFDTRA GFVGEYVNFV REDSVQGQRI DLRPYLRTER EGAAWFARGQ LGYDYTTYKL
TDTDFSPGQS TDPSRSLPTF SAEYGLRFER ITGSNQLQLL EPRVFYLYTP YENQDDQPVF
DGGEPDFEFT QLFSQNRFLG RDRVSDANHV AIATTLRQLD PDSGVTRFSA SIGQLFRFQA
PRVTLPDGTA PDSGATDFIA SLDYRISEKL RTVMAAQWSP SENEFNRTSF GFSYRSDRRR
LDLGYRYREN QLEQTDVILS TPLWQRWSAA GRWRYSLEDE QTLDTQAGLQ YETCCWALRT
SYRRYIATTS GDFSSGIYVQ LALKGLGQIG SGSGLLQSDS DFYE
//