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Penicillin-binding protein 1A (PBP-1a) (PBP1a) (Penicillin-binding protein A) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPA_HAEIN              Reviewed;         853 AA.
P31776;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
22-NOV-2017, entry version 131.
RecName: Full=Penicillin-binding protein 1A;
Short=PBP-1a;
Short=PBP1a;
AltName: Full=Penicillin-binding protein A;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000250|UniProtKB:P02918};
AltName: Full=Peptidoglycan TGase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000250|UniProtKB:P02918};
AltName: Full=DD-transpeptidase;
Name=mrcA; Synonyms=ponA; OrderedLocusNames=HI_0440;
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
Pasteurellaceae; Haemophilus.
NCBI_TaxID=71421;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=1916268; DOI=10.1016/0378-1119(91)90457-M;
Tomb J.-F., El-Hajj H., Smith H.O.;
"Nucleotide sequence of a cluster of genes involved in the
transformation of Haemophilus influenzae Rd.";
Gene 104:1-10(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800; DOI=10.1126/science.7542800;
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae
Rd.";
Science 269:496-512(1995).
[3]
CHARACTERIZATION.
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7592463; DOI=10.1128/jb.177.23.6745-6750.1995;
Sharma U.K., Dwarakanath P., Banerjee N., Town C., Balganesh T.S.;
"Expression and characterization of the ponA (ORF I) gene of
Haemophilus influenzae: functional complementation in a heterologous
system.";
J. Bacteriol. 177:6745-6750(1995).
[4]
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=10675023;
DOI=10.1002/(SICI)1522-2683(20000101)21:2<411::AID-ELPS411>3.0.CO;2-4;
Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B.,
Gray C., Fountoulakis M.;
"Two-dimensional map of the proteome of Haemophilus influenzae.";
Electrophoresis 21:411-429(2000).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000250|UniProtKB:P02918}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000250|UniProtKB:P02918}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-
pass type II membrane protein {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M62809; AAA25007.1; -; Genomic_DNA.
EMBL; L42023; AAC22099.1; -; Genomic_DNA.
PIR; D64068; JH0438.
RefSeq; NP_438601.1; NC_000907.1.
RefSeq; WP_005693721.1; NC_000907.1.
PDB; 5U2G; X-ray; 2.61 A; A/B=32-853.
PDBsum; 5U2G; -.
ProteinModelPortal; P31776; -.
SMR; P31776; -.
STRING; 71421.HI0440; -.
CAZy; GT51; Glycosyltransferase Family 51.
EnsemblBacteria; AAC22099; AAC22099; HI_0440.
GeneID; 949537; -.
KEGG; hin:HI0440; -.
PATRIC; fig|71421.8.peg.460; -.
eggNOG; ENOG4108JQC; Bacteria.
eggNOG; COG5009; LUCA.
KO; K05366; -.
OMA; LAQMAMI; -.
UniPathway; UPA00219; -.
Proteomes; UP000000579; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
Gene3D; 1.10.3810.10; -; 1.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR031376; PCB_OB.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF17092; PCB_OB; 1.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 4.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Carboxypeptidase;
Cell inner membrane; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 853 Penicillin-binding protein 1A.
/FTId=PRO_0000083165.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 853 Periplasmic. {ECO:0000255}.
REGION 37 205 Transglycosylase.
REGION 387 681 Transpeptidase.
ACT_SITE 75 75 Proton donor; for transglycosylase
activity. {ECO:0000250|UniProtKB:P02919}.
ACT_SITE 441 441 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000250|UniProtKB:P02919}.
CONFLICT 33 33 L -> LPSVETLKTVEL (in Ref. 1).
{ECO:0000305}.
STRAND 37 40 {ECO:0000244|PDB:5U2G}.
STRAND 46 50 {ECO:0000244|PDB:5U2G}.
HELIX 65 74 {ECO:0000244|PDB:5U2G}.
HELIX 146 155 {ECO:0000244|PDB:5U2G}.
STRAND 162 164 {ECO:0000244|PDB:5U2G}.
HELIX 165 171 {ECO:0000244|PDB:5U2G}.
HELIX 182 190 {ECO:0000244|PDB:5U2G}.
HELIX 191 193 {ECO:0000244|PDB:5U2G}.
TURN 195 197 {ECO:0000244|PDB:5U2G}.
TURN 200 202 {ECO:0000244|PDB:5U2G}.
HELIX 204 220 {ECO:0000244|PDB:5U2G}.
HELIX 226 233 {ECO:0000244|PDB:5U2G}.
HELIX 251 265 {ECO:0000244|PDB:5U2G}.
HELIX 267 272 {ECO:0000244|PDB:5U2G}.
STRAND 276 280 {ECO:0000244|PDB:5U2G}.
HELIX 283 302 {ECO:0000244|PDB:5U2G}.
STRAND 310 313 {ECO:0000244|PDB:5U2G}.
HELIX 322 331 {ECO:0000244|PDB:5U2G}.
STRAND 338 346 {ECO:0000244|PDB:5U2G}.
STRAND 348 358 {ECO:0000244|PDB:5U2G}.
STRAND 360 365 {ECO:0000244|PDB:5U2G}.
HELIX 366 371 {ECO:0000244|PDB:5U2G}.
STRAND 372 374 {ECO:0000244|PDB:5U2G}.
STRAND 381 387 {ECO:0000244|PDB:5U2G}.
STRAND 393 396 {ECO:0000244|PDB:5U2G}.
STRAND 400 409 {ECO:0000244|PDB:5U2G}.
TURN 410 412 {ECO:0000244|PDB:5U2G}.
STRAND 414 419 {ECO:0000244|PDB:5U2G}.
TURN 424 426 {ECO:0000244|PDB:5U2G}.
TURN 431 433 {ECO:0000244|PDB:5U2G}.
HELIX 440 443 {ECO:0000244|PDB:5U2G}.
HELIX 444 454 {ECO:0000244|PDB:5U2G}.
STRAND 461 465 {ECO:0000244|PDB:5U2G}.
STRAND 482 484 {ECO:0000244|PDB:5U2G}.
STRAND 488 491 {ECO:0000244|PDB:5U2G}.
HELIX 492 497 {ECO:0000244|PDB:5U2G}.
HELIX 501 511 {ECO:0000244|PDB:5U2G}.
HELIX 513 520 {ECO:0000244|PDB:5U2G}.
HELIX 521 523 {ECO:0000244|PDB:5U2G}.
HELIX 527 529 {ECO:0000244|PDB:5U2G}.
HELIX 534 538 {ECO:0000244|PDB:5U2G}.
STRAND 541 543 {ECO:0000244|PDB:5U2G}.
HELIX 545 557 {ECO:0000244|PDB:5U2G}.
STRAND 567 571 {ECO:0000244|PDB:5U2G}.
STRAND 577 580 {ECO:0000244|PDB:5U2G}.
HELIX 676 691 {ECO:0000244|PDB:5U2G}.
HELIX 703 707 {ECO:0000244|PDB:5U2G}.
STRAND 712 720 {ECO:0000244|PDB:5U2G}.
STRAND 724 733 {ECO:0000244|PDB:5U2G}.
STRAND 736 743 {ECO:0000244|PDB:5U2G}.
HELIX 757 760 {ECO:0000244|PDB:5U2G}.
HELIX 762 773 {ECO:0000244|PDB:5U2G}.
STRAND 787 792 {ECO:0000244|PDB:5U2G}.
TURN 794 796 {ECO:0000244|PDB:5U2G}.
STRAND 801 803 {ECO:0000244|PDB:5U2G}.
STRAND 805 810 {ECO:0000244|PDB:5U2G}.
TURN 811 813 {ECO:0000244|PDB:5U2G}.
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


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