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Database: UniProt
Entry: A0A2T7UXJ9_9RHOB
LinkDB: A0A2T7UXJ9_9RHOB
Original site: A0A2T7UXJ9_9RHOB 
ID   A0A2T7UXJ9_9RHOB        Unreviewed;       649 AA.
AC   A0A2T7UXJ9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:PVE49364.1};
GN   Name=mrdA {ECO:0000313|EMBL:PVE49364.1};
GN   ORFNames=DDE23_02880 {ECO:0000313|EMBL:PVE49364.1};
OS   Pararhodobacter aggregans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pararhodobacter.
OX   NCBI_TaxID=404875 {ECO:0000313|EMBL:PVE49364.1, ECO:0000313|Proteomes:UP000244810};
RN   [1] {ECO:0000313|EMBL:PVE49364.1, ECO:0000313|Proteomes:UP000244810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-19 {ECO:0000313|EMBL:PVE49364.1,
RC   ECO:0000313|Proteomes:UP000244810};
RX   PubMed=21959289; DOI=10.1016/j.syapm.2011.08.006;
RA   Foesel B.U., Drake H.L., Schramm A.;
RT   "Defluviimonas denitrificans gen. nov., sp. nov., and Pararhodobacter
RT   aggregans gen. nov., sp. nov., non-phototrophic Rhodobacteraceae from the
RT   biofilter of a marine aquaculture.";
RL   Syst. Appl. Microbiol. 34:498-502(2011).
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:PVE49364.1}.
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DR   EMBL; QDDR01000001; PVE49364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7UXJ9; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000244810; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244810}.
FT   DOMAIN          63..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"
SQ   SEQUENCE   649 AA;  70893 MW;  7A94B8AE64D18B30 CRC64;
     MKRPPKDNED SARVISRRAM LMGGAQMVFA GALVLRMRNL QLGQAEEFRL LADENRINIR
     LLPPSRGLIV DRNGTLLAGN VQNYRIVLVR EDAGEPRAAL ERLAQLIPLS PDEIDRAERE
     IMRHRPFVPV TIVDQLNWEE VARVAANAPA MPGITPEVGF NRHYPFGAEF AHSVGYVGPV
     SEADLAARET PEPLLMIPRF QIGKIGVERE YEETLRGTAG HRRVEVNAVG REMRELDRQE
     GDPGSTLQLT LDRQLQAFTL ARLGEDSAAA VVLEVQTGNV LALASAPSFD PNLFVRGISV
     ADYGALRDND HRPMSNKTVQ GAYPPGSTFK MVTALAAFEA GLATPDERVY CPGYIEAAGR
     RFHCWNRGGH GRVNLTSALS ESCDVFFYDM AQRVGIDRIN AMAERLGLGI RYDLPLSGIS
     SGLNPSREWK RERRGAEWVV GDTINASIGQ GYVLATPLQL AVMTARLATN RAILPRLIHA
     IDDIEQPIPD QPPLGLSAAA LAQVQRGMWE VSNAQRGTAY GSRIVDANLR MAGKTGSSQV
     FSITAAERAA GVRRQDQLPW NRRDHALFVC YAPDTDPRYA VSVVVEHGGG GSSVAAPIAR
     DIILAAQSGG LPPIEAYPQP QRNRIETMMR TISEQIGPAV APPTGRSRA
//
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