ID A0A017HD26_9RHOB Unreviewed; 840 AA.
AC A0A017HD26;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=Lokhon_01201 {ECO:0000313|EMBL:EYD72402.1};
OS Limimaricola hongkongensis DSM 17492.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD72402.1, ECO:0000313|Proteomes:UP000025047};
RN [1] {ECO:0000313|EMBL:EYD72402.1, ECO:0000313|Proteomes:UP000025047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD72402.1,
RC ECO:0000313|Proteomes:UP000025047};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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 -!- 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:EYD72402.1}.
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DR EMBL; APGJ01000004; EYD72402.1; -; Genomic_DNA.
DR RefSeq; WP_026147459.1; NZ_KK088650.1.
DR AlphaFoldDB; A0A017HD26; -.
DR STRING; 1122180.Lokhon_01201; -.
DR PATRIC; fig|1122180.6.peg.1188; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000025047; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000025047};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 60..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 337..442
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 444..733
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 840 AA; 92128 MW; C988FC46EA28613A CRC64;
MLRFIMSFFG GIFSMLTLGL AMGALTLGAI FYVYGRDLPS YETLAQYTPP TISRVYDGEG
DILDEFASER RLFTPAAEIP DLVKHAFVSA EDQNFYVHGG FDIKGIGAAA VEAVRSRGQE
LRGASTITQQ VMKNFLLDGS RTVERKIKEL ILAVRIEGAM DKERILELYL NEIFLGQNSY
GVTAAAQSYF NKPLAQLEPG EAAYLAALAQ RPGNLHPVRQ YSDAVNRRNY VLRRMWEDGY
IDEAAYRDGR GRTLDTVQSG DIESFRAALP PRDYFTDEVR RQLSAEFGED EFFGGGLSIR
ATLDGELQIE AAHALQRALE QFDRGRGRWH GTGKSIPVET LDDEIAWRKA LSEVDVPRDV
TLESPWRPAV VMEIGDQDMR LGIEGLADDG SEPHVVPRDD ISWMRGSFAD NFERGDVVLV
RRMITDDGGD FIRWTLRQTP KVQGAFMAMD VNTGRVLAMQ GGFSYQDSVF NRATQAQRQP
GSSFKPFVYA AALDSGYTPA TIIVDAPIEI NTPQGMWRPQ NASNRFYGPT PLRTGIERSR
NIMTIRLAQE VGMDTVADYG ERFGVYDDLG PYLSNALGAQ ETTLFKMVAA YAMFANGGER
VEPTLVDRVQ DRYGNTVYRH DQRNCVDCGL AALPAGKAPT IQSNRERIMN AVTAYQLTSM
MQGVVERGTA RGINLPVPIA GKTGTTNDAK DVWFVGFSSN IVAGCYIGYD NPRSLGSGAS
GGGICGPVFE SFMKKAISRF GGTAFPVPEE CQFIKIDRFS GARLPDSASG DNVISECFRM
GEQPLFGVAF DGGFEMSGDL PLYEEAGGNK PAKNVRNSTG GTATVGPKAS FGTLSSGGLY
//
