ID A0A2K1EAA5_9SPHN Unreviewed; 637 AA.
AC A0A2K1EAA5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:PNQ77200.1};
GN Name=mrdA {ECO:0000313|EMBL:PNQ77200.1};
GN ORFNames=BA950_03905 {ECO:0000313|EMBL:PNQ77200.1};
OS Erythrobacter sp. SAORIC-644.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1869314 {ECO:0000313|EMBL:PNQ77200.1, ECO:0000313|Proteomes:UP000236145};
RN [1] {ECO:0000313|EMBL:PNQ77200.1, ECO:0000313|Proteomes:UP000236145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-644 {ECO:0000313|EMBL:PNQ77200.1,
RC ECO:0000313|Proteomes:UP000236145};
RA Song J., Kogure K.;
RT "Erythrobacter sp. SAORIC-644 genome sequencing.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:PNQ77200.1}.
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DR EMBL; POYF01000002; PNQ77200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1EAA5; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000236145; 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: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, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..235
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 268..594
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 637 AA; 69739 MW; 7416441A39CBB95B CRC64;
MCVAKPPTNK RILEQQFSRR ATILCAVQLG LGGVLAGRLA WLAIAENQKW QLLSESNRLQ
LSLIPPRRGL LLDRTGVPLA SNKSVFMIDL LPDRLEDADK VLKQLAELLD LSADETDRLK
TDLEQALDHQ PVRVASDVEW DQYAAVNVRL PDLPGVSPMR GFSRHYPAGA ATAHLLGYVG
APSREEYEKT GDPLLMVPGM QVGKDMLEKT LDEHLTGKPG ARRAEVTATG KVVRALEVRS
DTIGKSVQLT IDGGLQTYAS RRLGTQSGSV VVLDAVTGGV LAMASMPAYD PNSFSDGISQ
FEWDMLSQDE RVPLRNKTLQ GLYPPGSTIK PITALALLNE NIDPDETVLC TGRINIAGGT
FHCWRRSGHG VVDMNRAIAE SCDIYFYVMG IRVGIQPIAD MARRFGLGER FLGLPVPYQY
YGTVPDPAWK RRRYNEPWEA YDTVNATIGQ GYLLANPLQL AVMTARLAAG EKTHPKLLAA
KEAPAAPLEI DPRMLAIVRQ GMEDVVNGQG TATRARLPLP NIKLAGKTGT AQVRRITMAE
RRRGVRSNAS LPWKLRDHGL FVGYAPVHRP RYTVAVVIEH GGGSGAAYPI ASDTLLYLFD
ERQAMKRLAS LENGWGGGIE ERMAREAAEF AARTPSD
//
