ID H8LLW3_RICSL Unreviewed; 790 AA.
AC H8LLW3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=MC3_06900 {ECO:0000313|EMBL:AFD20229.1};
OS Rickettsia slovaca str. D-CWPP.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105109 {ECO:0000313|EMBL:AFD20229.1, ECO:0000313|Proteomes:UP000007592};
RN [1] {ECO:0000313|EMBL:AFD20229.1, ECO:0000313|Proteomes:UP000007592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D-CWPP (RSB) {ECO:0000313|Proteomes:UP000007592};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RL Submitted (MAR-2012) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003375; AFD20229.1; -; Genomic_DNA.
DR RefSeq; WP_014273826.1; NC_017065.1.
DR AlphaFoldDB; H8LLW3; -.
DR KEGG; rsw:MC3_06900; -.
DR PATRIC; fig|1105109.3.peg.1455; -.
DR HOGENOM; CLU_006354_2_4_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007592; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 GO; GO:0046677; P:response to antibiotic; 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; 2.
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 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; PF17092; PCB_OB; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 322..417
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 419..713
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 790 AA; 88815 MW; 622B0521930E66D4 CRC64;
MYKSLLFCLK IFVFLILVGC GITAYIIYHY SRDLPDYSQL ARYYPPSVTR IYSRDGKLME
EYAFERRVFV PINSVPSSLI ESFIAAEDKN FYNHPGFDLF GIVRAAFLNI SNYLHHRRME
GASTITQQVV KNFLLTNEVS LERKIKEAIL SYMISRVFTK DQILELYLNQ TFFGRGAYGV
AVAAQNYFNK SVEELTIAES AFIAALPKAP SELNPERNYA RVKARRDYVI ARMFEDGYIT
RDAAKEAMDS PIVLRKRAKE ETVTADYYAA QVREEVIRML NSKEEFYTGG LTIITSLDAK
MQQLAENSLR KGLREFDRRR GFRKPIANIS LDNWQGELKK LPTPPSLLEY KLAVVLDVAD
NHVEIGLIDG SKSKMPIAEM KWARSNFKSV KTLLKKGDVI VVEAIKEGYA LRQIPEVNGA
IMVMNPNTGQ VLASVGGYDF STSKFDRVTQ ALRQPGSLSK TFVYLAALEN GVKPNQIFND
GPIEISQGPG MPSWRPKNYE GKFLGEITMR TGLEKSRNLI TVRVATAVGL TKIVDIIKRF
GINNEPKKVY SMVLGSIETT LSRMTNAYAI IANGGKKVEP HFVELIKDRN GKIIYRRDDR
ECLACNVSDS NLDTAILEIP KEYIYRVTDE ASDYQITSFL TGAIDRGTGY AAKKLGKIIG
GKTGTSNDSK DTWFVGFTPK IVVGSYVGYD TPKELGKRAT GSNVVLPIFI DFMSNAYKDK
PSLPFKVPDS IKLIAVDSAT GKITPSGTVI EAFKVNNVQM LENEDMIDNQ DNNDIFDYVP
SKEDQSQEIY
//
