ID A0A1H8K3F8_9BURK Unreviewed; 177 AA.
AC A0A1H8K3F8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000256|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000256|HAMAP-Rule:MF_02204};
GN Name=pal {ECO:0000256|HAMAP-Rule:MF_02204};
GN ORFNames=SAMN05428959_103531 {ECO:0000313|EMBL:SEN87207.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN87207.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity. {ECO:0000256|HAMAP-
CC Rule:MF_02204}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer.
CC {ECO:0000256|HAMAP-Rule:MF_02204}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_02204}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_02204}.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000256|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; FODC01000003; SEN87207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8K3F8; -.
DR STRING; 1881038.SAMN05428959_103531; -.
DR OrthoDB; 9809164at2; -.
DR Proteomes; UP000198691; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; OmpA-like domain; 1.
DR HAMAP; MF_02204; Pal; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR039001; Pal.
DR InterPro; IPR014169; Pal_lipo_C.
DR NCBIfam; TIGR02802; Pal_lipo; 1.
DR PANTHER; PTHR30329:SF22; PEPTIDOGLYCAN ASSOCIATED LIPOPROTEIN; 1.
DR PANTHER; PTHR30329; STATOR ELEMENT OF FLAGELLAR MOTOR COMPLEX; 1.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; OmpA-like; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_02204};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02204};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_02204};
KW Reference proteome {ECO:0000313|Proteomes:UP000198691};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02204}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..177
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011651651"
FT DOMAIN 61..177
FT /note="OmpA-like"
FT /evidence="ECO:0000259|PROSITE:PS51123"
FT REGION 146..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 18323 MW; FBEA09D438FFA9F5 CRC64;
MNVKINTLLA ACTVALLSAC STPAPAPAPA PAPAPAPAAA PAPAPAPVAA PVAATLPAYL
DPNSSIYKNR SVYFDFDKYT VKPEFDAVVA DHGKFLAANP NVSIKVEGNT DDQGSAEYNL
ALGQKRAQAV ITALKTQGVK DTQMEAVSFG KEKPKASGTD ADSRAQNRRA DLAYPSK
//
