ID A0A095WZE9_9GAMM Unreviewed; 817 AA.
AC A0A095WZE9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=HRUBRA_01410 {ECO:0000313|EMBL:KGE04004.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE04004.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE04004.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE04004.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
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 -!- 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:KGE04004.1}.
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DR EMBL; AUVB01000041; KGE04004.1; -; Genomic_DNA.
DR RefSeq; WP_035517883.1; NZ_KN234791.1.
DR AlphaFoldDB; A0A095WZE9; -.
DR STRING; 1265313.HRUBRA_01410; -.
DR PATRIC; fig|1265313.6.peg.1394; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029640; 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: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:0000313|EMBL:KGE04004.1};
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:UP000029640};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:KGE04004.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 54..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 348..441
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 446..708
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 790..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 817 AA; 89288 MW; 96FFD0FA86F96A3D CRC64;
MTFLRRLTRL ALLGSLGLVW LLAGVYLYLG PGLPEVETLR DVQLQTPMRV YTADGELIGQ
FGEQKRNPLA YDNIPSQFID ALLAAEDDGF FEHGGIDFMG LARAVTELLM TGQKRSGGST
LTMQVARNYF LSLERTFLRK FKEILLAIEI ERRLSKEEIF ELYFNRVFLG HRAYGFEAAA
QVYYGKGIGE LTLAQHAMLA GIPKAPSRDN PLSGPEAGRE RRNWILGRML NLGYIDRTAY
EASVRAPVTA DHYGPQVSFD ARYVAEMARK QMLERFGSAA YTAGYEVHTT LRSDLQRVAQ
RAVIAGLRTY DRRHGYRGPE LELPVPETLA AADAAEDPNN LPPAPPLPRD EWLDVLAELP
AVAGLTAAAV TTVDADRVHI LLADGSEAVV LWENGLRQAR PYLSENAVGG APESPAEVLS
VGDVIRVDRE GGAWHLAQVP AAQAALVSLA PDDGAILSLV GGIGFELSKF NRATQAERQP
GSNFKPFLYA AALDAGYTAA SIINDAPIVM EDASLEGLWR PENDGGKFYG PTRLRWALTK
SRNLVSIRLL RQLGVRRLIA YAGQLGFDTG DFAPDLSLAL GTHAMAPLEL AAAYAVLANG
GYRVEPYLIA RVDDSAGNTV WAADPPRVCR DCAGRELSME EILAGENANG HRRAERVMDE
RVNFILDDML QDVITRGTGR RALALKRKDL AGKTGTTNGP MDAWFSGYNR DVVTTTWVGF
DAYTPLGRRE FGGTAALPIW IDFMRAALAD SPDRERPVPA GIASVRIDPQ SGRRTGAGDG
DAIFEYFREE NVPASTEDGS ENTPGKTGTD ELIRDIF
//
