ID F9U6H1_9GAMM Unreviewed; 869 AA.
AC F9U6H1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=LPS-assembly protein LptD {ECO:0000256|HAMAP-Rule:MF_01411};
DE Flags: Precursor;
GN Name=lptD {ECO:0000256|HAMAP-Rule:MF_01411};
GN ORFNames=ThimaDRAFT_0522 {ECO:0000313|EMBL:EGV19847.1};
OS Thiocapsa marina 5811.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocapsa.
OX NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV19847.1, ECO:0000313|Proteomes:UP000005459};
RN [1] {ECO:0000313|EMBL:EGV19847.1, ECO:0000313|Proteomes:UP000005459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5811 {ECO:0000313|EMBL:EGV19847.1,
RC ECO:0000313|Proteomes:UP000005459};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA Bryant D., Woyke T.J.;
RT "The draft genome of Thiocapsa marina 5811.";
RL Submitted (JUN-2011) 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}.
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DR EMBL; AFWV01000002; EGV19847.1; -; Genomic_DNA.
DR AlphaFoldDB; F9U6H1; -.
DR STRING; 768671.ThimaDRAFT_0522; -.
DR PATRIC; fig|768671.3.peg.572; -.
DR eggNOG; COG1452; Bacteria.
DR Proteomes; UP000005459; 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 Gene3D; 2.60.450.10; Lipopolysaccharide (LPS) transport protein A like domain; 1.
DR HAMAP; MF_01411; LPS_assembly_LptD; 1.
DR InterPro; IPR020889; LipoPS_assembly_LptD.
DR InterPro; IPR045659; LptD_2.
DR InterPro; IPR007543; LptD_C.
DR InterPro; IPR005653; OstA-like_N.
DR PANTHER; PTHR30189; LPS-ASSEMBLY PROTEIN; 1.
DR PANTHER; PTHR30189:SF1; LPS-ASSEMBLY PROTEIN LPTD; 1.
DR Pfam; PF04453; LptD; 1.
DR Pfam; PF19838; LptD_2; 1.
DR Pfam; PF03968; LptD_N; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_01411};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01411};
KW Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01411}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT CHAIN 20..869
FT /note="LPS-assembly protein LptD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01411"
FT /id="PRO_5009012528"
FT DOMAIN 179..255
FT /note="Organic solvent tolerance-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03968"
FT DOMAIN 320..400
FT /note="LPS-assembly protein LptD central"
FT /evidence="ECO:0000259|Pfam:PF19838"
FT DOMAIN 421..788
FT /note="LptD C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04453"
FT REGION 29..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 96089 MW; 0462146B46AE2666 CRC64;
MHLVSLAIIL CAVAATAVAD DRSAAETNAA AEAAASPGLA LDPTEHPDDT SADAPDAAPD
AATGAPGAAS SSPASVAVPV PLPPLEPLMR HTPSEALQDL DRPDPQGDSD AVLPLLVSPE
DPGATAPTVE FAPRALELPA AWDPRLHADL PWEFCGPRSG AAGFAGPAAP AGTAGVPVNI
VADRVDYDRN TEVIQLRGGV DVVQADQRLS ADRSNYDRRS GRLDASGNVF LETPGLRIQG
DTADYNVLTR QGTIDAARYR LSGSANLLGT AEEAEILSEQ QSRYRNITYT TCPPGNADWS
IRARDLKLDQ EAGMGYAHHA RIRIGKIPVL YTPYIFFPID DRRRSGFLIP SFGSSDKTGT
DISIPYYWNI APNIDATITP RIMSTRGLML GTQLRYLDRF QQVEINAEVL PEDRRATELG
TRGAVRIEQT GQLGPRWSSA IDFTSVSDDE YLQDFGNRLD TTSLRNLVQR GDVNYFGKGW
RALARVQQFQ TVDAAIAPAN RPYGQLPHIE LDLNRRRWND LVEYDLEGQY DFFDNSARVY
GNRLVAVPTL RLPLRRSFGH LIPRARLYYT GYDLLNQAEG LPSRQSYAIP SFDLDGLLVF
ERDTGWFGTP TLQTLEPRIY YVLTSFEDQS NAPLFDTTEL DFSFASLFRP NRFTGYDRIG
DENRLTLGLT SRTIANQTGR ELFRASLGQI YYFEDRRVQL SADTVEDDIR SSVAGEFAAR
VTDDWSARAS LQWNPNDTEA PWEKRVVQLR YAREEGSRLN LAYRFNDGDD PDLRYEDTDI
SLQVPIGPQV KLVGRWLYSI LNEETVEAFA GIEFGRCCWR LRLLGQHLQT GSDSGSTSLM
LQVELAGLGS FGNQIDTLLE RGIYGYHSD
//
