LPOA_HAEIN
ID LPOA_HAEIN Reviewed; 575 AA.
AC P45299;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Penicillin-binding protein activator LpoA;
DE Short=PBP activator LpoA;
DE Flags: Precursor;
GN Name=lpoA; OrderedLocusNames=HI_1655;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 256-573, AND DISULFIDE BOND.
RX PubMed=18412262; DOI=10.1002/prot.22033;
RA Vijayalakshmi J., Akerley B.J., Saper M.A.;
RT "Structure of YraM, a protein essential for growth of Haemophilus
RT influenzae.";
RL Proteins 73:204-217(2008).
CC -!- FUNCTION: Regulator of peptidoglycan synthesis that is essential for
CC the function of penicillin-binding protein 1A (PBP1a). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PBP1a. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LpoA family. {ECO:0000305}.
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DR EMBL; L42023; AAC23299.1; -; Genomic_DNA.
DR PIR; B64174; B64174.
DR RefSeq; NP_439797.1; NC_000907.1.
DR RefSeq; WP_005694381.1; NC_000907.1.
DR PDB; 3CKM; X-ray; 1.35 A; A=256-573.
DR PDB; 4P29; X-ray; 1.95 A; A/B=33-253.
DR PDB; 5KCN; X-ray; 1.97 A; A=33-575.
DR PDB; 5VAT; X-ray; 2.60 A; A/B=33-575.
DR PDB; 5VBG; X-ray; 2.80 A; A=33-575.
DR PDB; 6DCJ; X-ray; 1.35 A; A/B=33-253.
DR PDBsum; 3CKM; -.
DR PDBsum; 4P29; -.
DR PDBsum; 5KCN; -.
DR PDBsum; 5VAT; -.
DR PDBsum; 5VBG; -.
DR PDBsum; 6DCJ; -.
DR AlphaFoldDB; P45299; -.
DR SMR; P45299; -.
DR STRING; 71421.HI_1655; -.
DR PRIDE; P45299; -.
DR EnsemblBacteria; AAC23299; AAC23299; HI_1655.
DR KEGG; hin:HI_1655; -.
DR PATRIC; fig|71421.8.peg.1733; -.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_026091_1_1_6; -.
DR OMA; MRLYAMG; -.
DR PhylomeDB; P45299; -.
DR BioCyc; HINF71421:G1GJ1-1672-MON; -.
DR EvolutionaryTrace; P45299; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0031241; C:periplasmic side of cell outer membrane; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell shape; Disulfide bond; Lipoprotein;
KW Membrane; Palmitate; Peptidoglycan synthesis; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..575
FT /note="Penicillin-binding protein activator LpoA"
FT /id="PRO_0000169453"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT DISULFID 356..554
FT /evidence="ECO:0000269|PubMed:18412262"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 168..184
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:6DCJ"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:6DCJ"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3CKM"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 441..451
FT /evidence="ECO:0007829|PDB:3CKM"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 475..480
FT /evidence="ECO:0007829|PDB:3CKM"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5KCN"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:3CKM"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 511..528
FT /evidence="ECO:0007829|PDB:3CKM"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:3CKM"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:3CKM"
SQ SEQUENCE 575 AA; 63437 MW; 3FCF093B22C56326 CRC64;
MSILLQGERF KKRLMPILLS MALAGCSNLL GSNFTQTLQK DANASSEFYI NKLGQTQELE
DQQTYKLLAA RVLIRENKVE QSAALLRELG ELNDAQKLDR ALIEARISAA KNANEVAQNQ
LRALDLNKLS PSQKSRYYET LAIVAENRKD MIEAVKARIE MDKNLTDVQR HQDNIDKTWA
LLRSANTGVI NNASDEGNAA LGGWLTLIKA YNDYIRQPVQ LSQALQSWKN AYPNHAAATL
FPKELLTLLN FQQTNVSQIG LLLPLSGDGQ ILGTTIQSGF NDAKGNSTIP VQVFDTSMNS
VQDIIAQAKQ AGIKTLVGPL LKQNLDVILA DPAQIQGMDV LALNATPNSR AIPQLCYYGL
SPEDEAESAA NKMWNDGVRN PLVAMPQNDL GQRVGNAFNV RWQQLAGTDA NIRYYNLPAD
VTYFVQENNS NTTALYAVAS PTELAEMKGY LTNIVPNLAI YASSRASASA TNTNTDFIAQ
MNGVQFSDIP FFKDTNSPQY QKLAKSTGGE YQLMRLYAMG ADAWLLINQF NELRQVPGYR
LSGLTGILSA DTNCNVERDM TWYQYQDGAI VPVAN
