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Database: UniProt
Entry: A0A1Q2SPC6_9GAMM
LinkDB: A0A1Q2SPC6_9GAMM
Original site: A0A1Q2SPC6_9GAMM 
ID   A0A1Q2SPC6_9GAMM        Unreviewed;       468 AA.
AC   A0A1Q2SPC6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Lipopolysaccharide export system protein LptA {ECO:0000256|HAMAP-Rule:MF_01914};
GN   Name=lptA {ECO:0000256|HAMAP-Rule:MF_01914};
GN   ORFNames=TAO_1620 {ECO:0000313|EMBL:BAW80990.1};
OS   Candidatus Nitrosoglobus terrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Candidatus Nitrosoglobus.
OX   NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW80990.1, ECO:0000313|Proteomes:UP000243679};
RN   [1] {ECO:0000313|EMBL:BAW80990.1, ECO:0000313|Proteomes:UP000243679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAO100 {ECO:0000313|EMBL:BAW80990.1,
RC   ECO:0000313|Proteomes:UP000243679};
RX   PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA   Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA   Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT   "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL   ISME J. 11:1130-1141(2017).
CC   -!- FUNCTION: Involved in the assembly of lipopolysaccharide (LPS).
CC       Required for the translocation of LPS from the inner membrane to the
CC       outer membrane. May form a bridge between the inner membrane and the
CC       outer membrane, via interactions with LptC and LptD, thereby
CC       facilitating LPS transfer across the periplasm. {ECO:0000256|HAMAP-
CC       Rule:MF_01914}.
CC   -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC       complex. {ECO:0000256|HAMAP-Rule:MF_01914}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01914}.
CC   -!- SIMILARITY: Belongs to the LptA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01914}.
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DR   EMBL; AP014836; BAW80990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2SPC6; -.
DR   KEGG; ntt:TAO_1620; -.
DR   OrthoDB; 9795964at2; -.
DR   Proteomes; UP000243679; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
DR   GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0015920; P:lipopolysaccharide transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.450.10; Lipopolysaccharide (LPS) transport protein A like domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   HAMAP; MF_01914; LPS_assembly_LptA; 1.
DR   InterPro; IPR014340; LptA.
DR   InterPro; IPR005653; OstA-like_N.
DR   NCBIfam; TIGR03002; outer_YhbN_LptA; 1.
DR   PANTHER; PTHR36504; LIPOPOLYSACCHARIDE EXPORT SYSTEM PROTEIN LPTA; 1.
DR   PANTHER; PTHR36504:SF1; LIPOPOLYSACCHARIDE EXPORT SYSTEM PROTEIN LPTA; 1.
DR   Pfam; PF03968; LptD_N; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01914};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243679};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01914}.
FT   DOMAIN          36..145
FT                   /note="Organic solvent tolerance-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03968"
FT   REGION          151..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  53079 MW;  FD6B4ADD70FFAE1F CRC64;
     MPQQISLRLI IFWLITQNLA YETALAFSND SGQPIHIEAD RGELDNRKQV AIYYGNVHLT
     QDNLRIDSDT LTIFYTPEKK IKKAIAEGQP AWYRQQSNDD SEDMRAKALK IEYHADNATI
     YLFQKAHVWQ GTNEFTGDRI VYDTEHRIVR GQGSKAGSGR VHVTIRPDEV EPSPNNSNST
     PKNSDSTPSL AAPPKNQVAD NQQLKSGEDQ GRTTDWLALY DSANIKSNQI ILLQPRTQVT
     IINRKDEWLH ITTLIKGELL EGWVEKKFIR LPESNTDSIS SSPIPIESSK NQVVKNQKSE
     SRQAQNRTTD WLNLYASTDI KSNKVARLQP QTQVTIIDRK DEWLYITALV EGELLEGWAE
     KKFIQLPETS MNSTHPSPIP IESSKNQIVK NQKIEIGQDR GRTADWLSLY ASANIKSNKV
     ALLQPHTQIT IIDRKGAWIY LTALVEGELL EGWAEGRFIQ LLESSQPK
//
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