LPOA_VIBAE
ID LPOA_VIBAE Reviewed; 603 AA.
AC D0M814;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 51.
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=VEA_004501;
OS Vibrio antiquarius (strain Ex25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio diabolicus subgroup.
OX NCBI_TaxID=150340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ex25;
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RT "Sequence of the deep-sea isolate Vibrio sp. strain Ex25.";
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACY52659.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001805; ACY52659.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006743240.1; NZ_DS267860.1.
DR AlphaFoldDB; D0M814; -.
DR SMR; D0M814; -.
DR KEGG; vex:VEA_004501; -.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cell shape; Lipoprotein; Membrane; Palmitate;
KW Peptidoglycan synthesis; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT CHAIN 25..603
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000405951"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01890"
SQ SEQUENCE 603 AA; 67673 MW; 1D71EBF52AA557F9 CRC64;
MINHKRLSVP RILTPVALAI TLAACSSGPR QPDGVDVTLE PTQSVQNYMI QADSTEGSLR
NDWLIMATKA AIQANQFDQA ELLIKRLARQ QLTEVQQAEW QLARATIQQK QGNYSQLLQL
LNFKPWWKLP NEQWKDYYLM RADAYQGLNQ AFEANRQLVA FGQYASSAEQ REISSRIWMN
FGSYSEYELT SLETEPNEDV LDGWLQLAVY AKTLSGNLSQ LKNTLERWLS ENPSHPAAIY
TPEEIQNILS LDIVKPNNTA LLLPLTGKFS PQAQLIRDGF VFAMMNDRNR DPSATLTVID
TNAYNADQIK QRLINKNIDF VVGPLEKENV ELLHTTMDGS ANGPTIPALA LNIPEDVQPD
SNICYLALSP EQEAAQAAKH LFSEGYNFPL ILAPKGSFGE RVTEAFNKEW RKYSSNKVAA
SYFGDKRQLQ KDINEVFGLQ ESKQRIAQMQ SLMRIKLETQ PRSRRDVDAV YIVARSTELT
LIKPFIEVAI NPDAKAPQIF SSSRSNSGGA TYEDLTGIIY SDIPLLIDPD PSVTAEMNEL
WSEQSNMEKR LKALGMDAYK LIGELPQMKV VPGYSVGGQT GILSIDNNCV VQRELSWAER
GAL