LPOA_PECPW
ID LPOA_PECPW Reviewed; 672 AA.
AC D0KEP3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=Pecwa_0314;
OS Pectobacterium parmentieri (strain WPP163) (Pectobacterium wasabiae (strain
OS WPP163)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WPP163;
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 Pectobacterium wasabiae WPP163.";
RL Submitted (OCT-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; CP001790; ACX86167.1; -; Genomic_DNA.
DR RefSeq; WP_012822118.1; NC_013421.1.
DR AlphaFoldDB; D0KEP3; -.
DR SMR; D0KEP3; -.
DR KEGG; pwa:Pecwa_0314; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
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..672
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405940"
FT REGION 298..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..336
FT /note="Polar residues"
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 672 AA; 72058 MW; AA99181BCFE2D63F CRC64;
MLPFHLVRTQ AGRVIPVLLA ALFLAGCPSH APQSPPPEVQ GKADASSDYY LQQMQQSSDN
NKADWQLLAI RSLLQEGKAP QASQQFNTLP EKLSAAQKQE QQLLSAELSA AQNNMDAAKA
ALSQLDVGAL SEQQKSRYYQ TQIKTAQGRP SIELLRAYIA QEPLLKGDEH QMNLDQTWLA
LTQMSPQESG ALLINADENV LQGWVDLLNN YQNNRESPDQ LQSAIQDWKT RYPHHPAAKN
LPMQLNQVIN YQPSSVSSIA LLLPLNGQAQ VFANAIQQGF NAAKNGQIAT AAVSAPVAPP
TDTAQAGQVT PSSDGQNAQS PAPYSDQAVA STTPAPAAQA TSAGLSSSLP VKVYDTSSQP
LANILTQAQQ DGASLVIGPL LKNEVDQLAS NPSPLNILAL NQPERVENSP NICYFALSPE
DEARDAAKFI HQQGKQQPLV LAPRGALGDR IVNAFAQAWN QQSGTSALQQ RFGNSAELKQ
AINSGAGLSL NGQPVNVSQQ QAQAGTTIGG LTIPSQVQPT ASSSVSGNID AVYIIATPDE
LALIKPMIDM RTSSRARPAL YASSRSFQAG LGPDFRLEME GLQFSDIPLL AGANPALMQQ
VSSQFKNDYS LVRLYAMGMD AWTLASHFGE MRQIPGHQIS GATGMLSAGP DCTINRQLTW
QQYRQGQLVP VL