LPOA_HISS2
ID LPOA_HISS2 Reviewed; 586 AA.
AC B0UTT2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=HSM_1207;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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; CP000947; ACA30931.1; -; Genomic_DNA.
DR RefSeq; WP_012340383.1; NC_010519.1.
DR AlphaFoldDB; B0UTT2; -.
DR SMR; B0UTT2; -.
DR STRING; 228400.HSM_1207; -.
DR EnsemblBacteria; ACA30931; ACA30931; HSM_1207.
DR KEGG; hsm:HSM_1207; -.
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; 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..586
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_5000311053"
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 586 AA; 66310 MW; A8A2CFA7EA0C3A26 CRC64;
MLSILMQGLR LKKCFLPILV MFFLAGCVNL LGSSFTASLK NDANASSDFY IRKIEQTQNQ
QDLQTYKLLA ARVLVTENKI PQAEAYLAEL IDLNDEQKLD KSLIEAHISA VKGKNETAEY
QLSLIHLTSL 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 YLINEE
