LPOA_SERP5
ID LPOA_SERP5 Reviewed; 674 AA.
AC A8GJZ0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Spro_4336;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) 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; CP000826; ABV43430.1; -; Genomic_DNA.
DR RefSeq; WP_012147033.1; NC_009832.1.
DR AlphaFoldDB; A8GJZ0; -.
DR SMR; A8GJZ0; -.
DR STRING; 399741.Spro_4336; -.
DR EnsemblBacteria; ABV43430; ABV43430; Spro_4336.
DR KEGG; spe:Spro_4336; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR OrthoDB; 776281at2; -.
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..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 32..674
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_5000279767"
FT REGION 291..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 32
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 32
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 674 AA; 72269 MW; F045927A135D71E6 CRC64;
MLSSTFVRTK AGRSKPVRLT AVIAAALFLA GCPSQAPQTP PANIQDEASA SSDYYLQQLQ
QSSNDNKADW QLLAIRALLR EGKLPQASEQ LNQLPKNLSS VQQVESQLLT AELQVANKSY
VSARSTLGHI DSGSLSANQL VRFYQAQIAV NQGKASLPLI RAYIAQEPLL TGKAHQNNLD
QTWQSLLQLT PQDMNSLVIN ANENVLQGWL DLLRVYQDNK QDPDLLKAGI KDWQNRYPQN
PAAKTLPTQL NQVLHFTQAS TSKIALLLPL NGQAKVFADA IQKGFEAAKN GVTPSTPVQQ
QQPASVPEQA AQPASTDPNA NGAVSTSAPD AAPVTAAQPS APSTAPITPP QAANAQIKVY
DTSSQPLAAL LTQAQQDGAT LVVGPLLKEN VDQLASSTTT LNVLALNQPE TPKDNPNICY
FALSPEDEAR DAARHIWEQQ KRQPLLLIPR GAFGDRVAKA FNQEWQKLGG QTVLQQGIGS
ASELRQMVNS GGIRMSGTPI STAPAPQAVT IAGLTIPAPP SDTPATSGGS VDSVYIVATQ
SQLTLIKPMI DMATNSRSKP AMYASSRSYQ AGAGPDFRLE MEGLQFSDIP LLAGANPQLL
QQASSQFRND YSLVRLYAMG MDAWTLSNHF AEMRQLPGFQ VSGTTGVLTA APGCVINRKL
PWLQYRQGTV VPVS