ID A0A2U3QGU8_9BACT Unreviewed; 766 AA.
AC A0A2U3QGU8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=NBG4_30015 {ECO:0000313|EMBL:SPQ00621.1};
OS Candidatus Sulfobium mesophilum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Sulfobium.
OX NCBI_TaxID=2016548 {ECO:0000313|EMBL:SPQ00621.1, ECO:0000313|Proteomes:UP000245125};
RN [1] {ECO:0000313|Proteomes:UP000245125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zecchin S.;
RL Submitted (MAR-2018) 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 -!- 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}.
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DR EMBL; OUUY01000075; SPQ00621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3QGU8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000245125; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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: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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR003029; S1_domain.
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 SMART; SM00316; S1; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000245125};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 343..422
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 766 AA; 84442 MW; F45754CC20AE912B CRC64;
MKFRLVIIFA VLSLLLGGIA GGYIAISKGI PSIEELKQYN QAAGTRIYAD DDVLIGELKI
EKGIFVSLDR MPKNIVNAIV AVEDSRFWKH KGIDYIAIAR AVVKDIIHAS LKEGGSTLTQ
QLAKVVFLSP EKTVKRKLME ASLAIQIENN LSKKEILELY LNKVYFGHGA YGVEMASKVY
FGKSVNHLTL AEASLIAGLV KAPTLYSPFN DLSRAKDRQA IVLARMEEEG YINKSERTTA
FAQPLYLASP KKGIEANSYF IDYIKKYLEE KYGLDTVYKG GMKVYTTLNR GMQSSAVAAV
QAGLKDVDKR RGWRGPLERK KDVDFEKELK AKELTGTVAI NPGDIYSGLV LKVSDKEAFI
KTRGVVGRLA IKDAMWASRT IMKEGAAKTI QNFSLSKILR PGDVIKVSIK SIQNKNIQLA
LEQDPEVEGA LVSVEPYTGF IRAMVGGYDF TRSDFNRAIL AKRQPGSAFK PVIYAAAMDN
GFTPASIIND EPASYVGGLK GEWNPENYDH KFYGPTRLRE ALAYSRNVVT VKLVDSMGID
NLINFARTVG FDGEIPRNLS IALGSLNITP FQLALVYDVF ASNGMKVRPI SIKYITDRKG
RVLESNEPNP EQTISPQTSF LITSMMQDVI KYGTGWRAKA LGVPVAGKTG TTNDYKDAWF
VGYSSGLVSC VWVGFDSFKT LGSLETGARA ASPIWVSFMQ NALHGNSEGF SQPEGIVTAV
IDPKTGLLSR DESGIREFFK DGSQPKQLSP SKSIWEVKEP QQIDFD
//
