ID F4D5Z7_HELPX Unreviewed; 659 AA.
AC F4D5Z7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Penicillin-binding protein, 1A family {ECO:0000313|EMBL:AEE70422.1};
GN ORFNames=HMPREF0462_0817 {ECO:0000313|EMBL:AEE70422.1};
OS Helicobacter pylori 83.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=585538 {ECO:0000313|EMBL:AEE70422.1, ECO:0000313|Proteomes:UP000008459};
RN [1] {ECO:0000313|EMBL:AEE70422.1, ECO:0000313|Proteomes:UP000008459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=83 {ECO:0000313|EMBL:AEE70422.1,
RC ECO:0000313|Proteomes:UP000008459};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00034000};
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:0000256|ARBA:ARBA00023988};
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP002605; AEE70422.1; -; Genomic_DNA.
DR RefSeq; WP_000913698.1; NC_017375.1.
DR AlphaFoldDB; F4D5Z7; -.
DR KEGG; hpx:HMPREF0462_0817; -.
DR PATRIC; fig|585538.3.peg.839; -.
DR HOGENOM; CLU_006354_2_4_7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008459; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
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; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 331..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 659 AA; 74137 MW; 463C58CD13E5A491 CRC64;
MLKKIFYGFI VLFLIVVGLL AILIAQVWVS TNKDIAKIKD YRPSVASQIL DRKGRLIANI
YDKEFRFYAR FEEIPPRFIE SLLAVEDTLF FEHGGINLDA IMRAMIKNAK SGRYTEGGST
LTQQLVKNMV LTREKTLTRK LKEAIISIRI EKVLSKEEIL ERYLNQTFFG HGYYGVKTAS
LGYFKKPLDK LTLKEITMLV ALPRAPSFYD PTKNLEFSLS RANDILRRLY SLGWISSNEL
KSALNEVPIV YNQTSTQNIA PYVVDEVLKQ LDQLDGLKTQ GYTIKLTIDL DYQRLALESL
RFGHQKILEK IAKEKPKTNA SNEDEDNLNA SMIVTDTSTG KILALVGGID YKKSAFNRAT
QAKRQFGSAI KPFVYQIAFD NGYSTTSKIP DTARNFENGN YSKNSEQNHA WHPSNYSRKF
LGLVTLQEAL SYSLNLATIN LSDQLGFEKI YQSLSDMGFK NLPKDLSIVL GSFAISPIEA
AEKYSLFSNY GTMLKPMLIE SITDQQNDIK TFTPIETKKI TSKEQAFLTL SVLMNAVENG
TGSLARIKGL EIAGKTGTSN NNIDAWFIGF TPTLQSVIWF GRDDNTPIGK GATGGVVSAP
VYSYFMRNIL AIEPSLKRKF DVPKGLRKEI VDKIPYYSTP NSITPTPQKT DDGEEPLLF
//
