ID A0A0S8EC95_9BACT Unreviewed; 769 AA.
AC A0A0S8EC95;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AMK74_00990 {ECO:0000313|EMBL:KPK46211.1};
OS Nitrospira bacterium SM23_35.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704026 {ECO:0000313|EMBL:KPK46211.1, ECO:0000313|Proteomes:UP000051169};
RN [1] {ECO:0000313|EMBL:KPK46211.1, ECO:0000313|Proteomes:UP000051169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_35 {ECO:0000313|EMBL:KPK46211.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK46211.1}.
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DR EMBL; LJUG01000007; KPK46211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EC95; -.
DR PATRIC; fig|1704026.3.peg.1192; -.
DR Proteomes; UP000051169; Unassembled WGS sequence.
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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 54..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 313..428
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 431..685
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 769 AA; 84669 MW; 42BD12A8D8F51080 CRC64;
MNRRLFISVA LISILLGVSA GGYVAYSMGI PSIEEIKQYK PTGGTKIYAD DDVIIGELKA
EKGTFVPLKN IPESIINAVV AVEDARFWKH KGIDYLAIAR ALFKDIIHGE LREGGSTITQ
QLAKVVFLTP EKTLQRKIRE AALAIKIEKN LDKREILELY LNKIYFGHGA YGVEMASRIY
FGKPVRDIKL PEAALITGLI KAPSLYSPFN DLGKARERQY IVLSRMVEEG YLKKSEMEQA
LKQPLSLSSM RKGIDANNYF IEYVRKYLED KYGIEKVYKG NLRVYTTLDR TAQTAAAKAV
QDGLRALDKR RGWRGPIDHK KDLDIGQEMK TSELSTIVAT NPGDLSTGLV LKVTNKEAIV
KVRGVIGKLA PEDAQWASKI LDLDSGKSRV LKKFILPQIL QPGDIVKVSI KSVQGNTIRL
SLQQEPQAEA ALVALDQETG FIRAMIGGYD FVKSDFNRVL YAKRQPGSAF KPIIYAAALQ
NGYTPASIIT DEPVTYTGGA QGDWSPENAD NKFHGPTTLR EALTYSRNVV TVKLVDAVGI
DKVVDFARTI GIQGELPRNL TLALGSLSIS PLELALCYSV FANGGLKVKP IAIKYITDAN
GSVLESNDPE AEEVISSTTA FLITSLMENV VQHGTGWRAK ALGRPVAGKT GTTNDYRDAW
FVGYTPNLTA AVWVGFDDTK PLGALETGAR AASPIWVSFM QNALSGPPEA FTVPEGIVIR
TIDPGTGLLA REEADGVREY FKEGTEPEQY TPSPFFRRIW KQDTNLNFD
//
