ID A0A1H7CKP2_9RHOB Unreviewed; 648 AA.
AC A0A1H7CKP2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:SEJ89814.1};
GN ORFNames=SAMN05444007_108156 {ECO:0000313|EMBL:SEJ89814.1};
OS Cribrihabitans marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cribrihabitans.
OX NCBI_TaxID=1227549 {ECO:0000313|EMBL:SEJ89814.1, ECO:0000313|Proteomes:UP000199379};
RN [1] {ECO:0000313|EMBL:SEJ89814.1, ECO:0000313|Proteomes:UP000199379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29340 {ECO:0000313|EMBL:SEJ89814.1,
RC ECO:0000313|Proteomes:UP000199379};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; FNYD01000008; SEJ89814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7CKP2; -.
DR STRING; 1227549.SAMN05444007_108156; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000199379; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000199379};
KW Transferase {ECO:0000313|EMBL:SEJ89814.1}.
FT DOMAIN 62..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 613..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71707 MW; 4C7D22A869BBF396 CRC64;
MKRNPRDIEA THRKLSRRAL LLGGAQAAFV GALAMRMRYM QVDQADQFRL LAEENRINIR
LIPPTRGELF DRNGVILGQN VPSYRIIIVR EDAGDVDKVI SDLSRLIELR PEDVERARAE
MRRSPPFLPI TLADRITWEE ISKVAVNAPA LPGITPEVGL TRVYPWQGDF AHVIGYVGPV
SDYDLSKMED PEPVLRIPRF QIGKVGLEAK REDILRGKAG AKRVEVNATG RVMRELDRQE
GQPGADLQMS VDAKLQHYVQ ARLGRESAAV VVMDCETGDL RAIASSPSFD PNLFVRGISV
ADYRGLTEDP YRPLANKTVQ GTYPPGSTFK MITAMAALEE GMIEPEETVY CPGFLKVGSR
RFHCWKRGGH GHVNLETSLK RSCDVYYYDL ALKVGIDRIS AMANRFGLGV RHELPMSAVA
DGLTPTQDWK QRVYGEGWLI GDTANASIGQ GFMLASPLQL AVMSARIATG REVAPRLVKS
INGIETPLIR GGSLGLNENN LRKMRKAMYA VSNDRRGTAY RSRIIAEGLR MAGKTGTSQV
RNITAAERAA GVISNEDLPW ERRDHALYVC FAPFEAPKYA VSVVVEHGGG GSRAAAPVAR
DVLLQALYDG TPPLEAYPKG DRSRIQAQQE RLQREDRPTL DTDGNDRA
//
