PBPA_HAEIN
ID PBPA_HAEIN Reviewed; 853 AA.
AC P31776;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Penicillin-binding protein 1A;
DE Short=PBP-1a;
DE Short=PBP1a;
DE AltName: Full=Penicillin-binding protein A;
DE Includes:
DE RecName: Full=Penicillin-insensitive transglycosylase;
DE EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=Peptidoglycan TGase;
DE Includes:
DE RecName: Full=Penicillin-sensitive transpeptidase;
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
DE AltName: Full=DD-transpeptidase;
GN Name=mrcA; Synonyms=ponA; OrderedLocusNames=HI_0440;
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 [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=1916268; DOI=10.1016/0378-1119(91)90457-m;
RA Tomb J.-F., El-Hajj H., Smith H.O.;
RT "Nucleotide sequence of a cluster of genes involved in the transformation
RT of Haemophilus influenzae Rd.";
RL Gene 104:1-10(1991).
RN [2]
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 [3]
RP CHARACTERIZATION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7592463; DOI=10.1128/jb.177.23.6745-6750.1995;
RA Sharma U.K., Dwarakanath P., Banerjee N., Town C., Balganesh T.S.;
RT "Expression and characterization of the ponA (ORF I) gene of Haemophilus
RT influenzae: functional complementation in a heterologous system.";
RL J. Bacteriol. 177:6745-6750(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000250|UniProtKB:P02918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000250|UniProtKB:P02918};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000305}.
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DR EMBL; M62809; AAA25007.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22099.1; -; Genomic_DNA.
DR PIR; D64068; JH0438.
DR RefSeq; NP_438601.1; NC_000907.1.
DR RefSeq; WP_005693721.1; NC_000907.1.
DR PDB; 5U2G; X-ray; 2.61 A; A/B=32-853.
DR PDBsum; 5U2G; -.
DR AlphaFoldDB; P31776; -.
DR SMR; P31776; -.
DR STRING; 71421.HI_0440; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PRIDE; P31776; -.
DR EnsemblBacteria; AAC22099; AAC22099; HI_0440.
DR KEGG; hin:HI_0440; -.
DR PATRIC; fig|71421.8.peg.460; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR PhylomeDB; P31776; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; -; 1.
DR Gene3D; 3.40.710.10; -; 3.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF17092; PCB_OB; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Carboxypeptidase; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..853
FT /note="Penicillin-binding protein 1A"
FT /id="PRO_0000083165"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..853
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 37..205
FT /note="Transglycosylase"
FT REGION 387..681
FT /note="Transpeptidase"
FT REGION 615..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Proton donor; for transglycosylase activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT ACT_SITE 441
FT /note="Acyl-ester intermediate; for transpeptidase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P02919"
FT CONFLICT 33
FT /note="L -> LPSVETLKTVEL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 204..220
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 348..358
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 545..557
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 676..691
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 703..707
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 712..720
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 724..733
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 736..743
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 757..760
FT /evidence="ECO:0007829|PDB:5U2G"
FT HELIX 762..773
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 794..796
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:5U2G"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:5U2G"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:5U2G"
SQ SEQUENCE 853 AA; 94221 MW; FC0846096CDB663B CRC64;
MRIAKLILNT LLTLCILGLV AGGMLYFHLK SELQQPMQIY TADGKLIGEV GEQRRIPVKL
ADVPQRLIDA FLATEDSRFY DHHGLDPIGI ARALFVAVSN GGASQGASTI TQQLARNFFL
TSEKTIIRKA REAVLAVEIE NTLNKQEILE LYLNKIFLGY RSYGVAAAAQ TYFGKSLNEL
TLSEMAIIAG LPKAPSTMNP LYSLKRSEER RNVVLSRMLD EKYISKEEYD AALKEPIVAS
YHGAKFEFRA DYVTEMVRQE MVRRFGEENA YTSGYKVFTT VLSKDQAEAQ KAVRNNLIDY
DMRHGYRGGA PLWQKNEAAW DNDRIVGFLR KLPDSEPFIP AAVIGIVKGG ADILLASGEK
MTLSTNAMRW TGRSNPVKVG EQIWIHQRAN GEWQLGQIPA ANSALVSLNS DNGAIEAVVG
GFSYEQSKFN RATQSLVQVG SSIKPFIYAA ALEKGLTLSS VLQDSPISIQ KPGQKMWQPK
NSPDRYDGPM RLRVGLGQSK NIIAIRAIQT AGIDFTAEFL QRFGFKRDQY FASEALALGA
ASFTPLEMAR AYAVFDNGGF LIEPYIIEKI QDNTGKDLFI ANPKIACIEC NDIPVIYGET
KDKINGFANI PLGENALKPT DDSTNGEELD QQPETVPELP ELQSNMTALK EDAIDLMAAA
KNASSKIEYA PRVISGELAF LIRSALNTAI YGEQGLDWKG TSWRIAQSIK RSDIGGKTGT
TNSSKVAWYA GFGANLVTTT YVGFDDNKRV LGRGEAGAKT AMPAWITYMK TALSDKPERK
LSLPPKIVEK NIDTLTGLLS PNGGRKEYFI AGTEPTRTYL SEMQERGYYV PTELQQRLNN
EGNTPATQPQ ELF
