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Database: UniProt
Entry: D4E9I0_SEROD
LinkDB: D4E9I0_SEROD
Original site: D4E9I0_SEROD 
ID   D4E9I0_SEROD            Unreviewed;       179 AA.
AC   D4E9I0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   ECO:0000313|EMBL:EFE93497.1};
GN   ORFNames=HMPREF0758_4830 {ECO:0000313|EMBL:EFE93497.1};
OS   Serratia odorifera DSM 4582.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE93497.1, ECO:0000313|Proteomes:UP000005723};
RN   [1] {ECO:0000313|EMBL:EFE93497.1, ECO:0000313|Proteomes:UP000005723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE93497.1,
RC   ECO:0000313|Proteomes:UP000005723};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2010) 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}.
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:EFE93497.1}.
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DR   EMBL; ADBY01000059; EFE93497.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4E9I0; -.
DR   STRING; 667129.HMPREF0758_4830; -.
DR   HOGENOM; CLU_016890_9_4_6; -.
DR   Proteomes; UP000005723; 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:UP000005723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02204}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..179
FT                   /note="Peptidoglycan-associated lipoprotein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003056400"
FT   DOMAIN          67..179
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51123"
FT   REGION          35..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   179 AA;  19493 MW;  259799FC65B00159 CRC64;
     MANYKRIKEM QLNKVLKGLL LALPVLAVAA CSSNKSADND QSGVGAGGTG MESGSSNLSS
     EEQARLQMQE LQKNNIVYFG LDKYDISSEF AQMLDAHATF LRNNPSYKVT VEGHADERGT
     PEYNIALGER RANAVKMYLQ GKGVSADQIS IVSYGKEKPA VLGHDEAAYS KNRRAVLVY
//
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