LPOA_DICC1
ID LPOA_DICC1 Reviewed; 682 AA.
AC C6CMD7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Penicillin-binding protein activator LpoA {ECO:0000255|HAMAP-Rule:MF_01890};
DE Short=PBP activator LpoA {ECO:0000255|HAMAP-Rule:MF_01890};
DE Flags: Precursor;
GN Name=lpoA {ECO:0000255|HAMAP-Rule:MF_01890}; OrderedLocusNames=Dd1591_3782;
OS Dickeya chrysanthemi (strain Ech1591) (Dickeya zeae (strain Ech1591)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=561229;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ech1591;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Dickeya zeae Ech1591.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC the function of penicillin-binding protein 1A (PBP1a).
CC {ECO:0000255|HAMAP-Rule:MF_01890}.
CC -!- SUBUNIT: Interacts with PBP1a. {ECO:0000255|HAMAP-Rule:MF_01890}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01890}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01890};
CC Periplasmic side {ECO:0000255|HAMAP-Rule:MF_01890}.
CC -!- SIMILARITY: Belongs to the LpoA family. {ECO:0000255|HAMAP-
CC Rule:MF_01890}.
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DR EMBL; CP001655; ACT08582.1; -; Genomic_DNA.
DR RefSeq; WP_015848091.1; NC_012912.1.
DR AlphaFoldDB; C6CMD7; -.
DR SMR; C6CMD7; -.
DR STRING; 561229.Dd1591_3782; -.
DR EnsemblBacteria; ACT08582; ACT08582; Dd1591_3782.
DR KEGG; dze:Dd1591_3782; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR Proteomes; UP000002735; Chromosome.
DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR HAMAP; MF_01890; LpoA; 1.
DR InterPro; IPR007443; LpoA.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR38038; PTHR38038; 1.
DR Pfam; PF04348; LppC; 2.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW Peptidoglycan synthesis; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 27..682
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405927"
FT REGION 240..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 682 AA; 72145 MW; 962A3E83087508B6 CRC64;
MLPLNSVRTH AGRLVPVMLA ALFLAGCPSQ APQSPAMQQR VEGKAGASSD YYLQQMQQSS
DDSKADWQLL AIHALIQEGK LPQAGNQLGT LPSQLGDKQR QEQRLLTAEL AVAQNDMNAA
NTMLAQLDVK SLSPQQQERY YQAQIKAAQD RTSLTLIRAY IGLEPLLQGD AHQRNIDQTW
TALTRLNQQD LSSMVINVDE NTLQGWLDLL NLWQTKAQVP SDLQAAIEDW KKRYPRHPAA
KQLPSQLGGT PPAAAAPTTG ETAPTGGNAI ALLLPLNGQA QAFANAIQQG FSAARSGQAS
LAMPAQPAQL AQAANNAAAA TPGAPAVPSP ASSTPSAVSP TPAAATTVMP ALTAATAGTI
PVKVYDTSNQ ALANVIAQAQ KDGATTIVGP LLKNEVEQLP GLNPSLNVLA LNQPEHIQPN
PNICYFALSP EDEAADAAQF IHKQGKQHPL ILAPRGNLGD RVVAAFAKSW QQQSGGVVLQ
QRTGSMYDLK QAINSGAGIP LNGQPVITAA SAPQPSTTVG GLTIPNQAPP IAAVTSDGNV
DAIYIIATPD ELALLKPMID MRNKGASRPA LYASSRSYQA GLGPDFRFEM EGLQFSDIPL
LTGASPALMQ QVSTQFRNDY SLVRLFAMGM DAWKLASDFS QLHQPGSSLS GATGILSASS
DCVVNRKLTW LQFRQGQLVP AS