LPOA_HAES1
ID LPOA_HAES1 Reviewed; 581 AA.
AC Q0I2P5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 70.
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}; Synonyms=lppC;
GN OrderedLocusNames=HS_0740;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI25015.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000436; ABI25015.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041604141.1; NC_008309.1.
DR AlphaFoldDB; Q0I2P5; -.
DR SMR; Q0I2P5; -.
DR STRING; 205914.HS_0740; -.
DR EnsemblBacteria; ABI25015; ABI25015; HS_0740.
DR KEGG; hso:HS_0740; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
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; 1.
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..581
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405935"
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 581 AA; 65702 MW; 7B816AB7CFEB5B11 CRC64;
MLSILMQGLR LKKCFLPILV MFFLAGCVNL LGSSFTASLK NDANASSDFY IRKIEQTQNQ
QDLQTYKLLA ARVLVTENKI PQAEAYLAEL IDLNDEQKLD KSLIEAHISA IKGKNETAEY
QLSLIHLTLL SPSQKSRYYE IVSRIAENRH DNISAIKARI QMDNFLSDIQ RKQQNNDRTW
ALLRNTDSEV LNNTDAEGNI TLSGWLTLAQ LYNDNLNQPA QLIQTLLTWK NYYPTHTAAH
LLPTELQGLA NFQQTTLTQV GLILPLSGNT RLIGETIKNG FDDAKVNYNV QVHVFDSMKM
SIEQIINQAK KQGINTLVGP LLKQNVDVIV NNPYLVQDLN VLALNSTPNA RAIEHLCYYG
LSPEDEAESA ASKMWNDTVR IPLVLVPQNN LGRRTAAAFT LRWQQLLGTD ANIKFYNQTA
DINFALKSGL SESTDGVYII ANNKQLAEIK AVLDNINPTL KLYASSRSNS PNSGPEHRLF
LNNLQFSDIP FFKDRESEQY KKIEKMTNND YSLMHLYAMG YDAWLLINQF NEFRQIPGFT
IDGLTGKLSA GPNCNVERDM TWFQYQNGSI YPLNEQDDSI I