ID A0A3N4M620_9BACT Unreviewed; 654 AA.
AC A0A3N4M620;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:RPD38784.1};
GN Name=mrdA {ECO:0000313|EMBL:RPD38784.1};
GN ORFNames=EG028_24080 {ECO:0000313|EMBL:RPD38784.1};
OS Chitinophaga barathri.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD38784.1, ECO:0000313|Proteomes:UP000279089};
RN [1] {ECO:0000313|Proteomes:UP000279089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) 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:RPD38784.1}.
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DR EMBL; RMBX01000014; RPD38784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4M620; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000279089; 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 Reference proteome {ECO:0000313|Proteomes:UP000279089};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..596
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 654 AA; 71949 MW; 104BC959217572D3 CRC64;
MSVFNQPRKR VIQLICLSMV TLIVVRLFYL QVVETKYSKL ADANAHLRKV IYPSRGIIYD
RKGRSVMRNE ALYDLMVTPR SVKNIDTGYL CEVLGIDKEE FIKRIANARM KEGPVRPSVF
ASLLTPEVYG KLQESMYMFQ PGFELVLRPV RSYPYGVGAN VFGYISEITP GMLNDSSGKY
SAYQQGDYIG MTGLERTYEN ILMGQRGIQY LVKDNLNRPQ GPLENGEFDT AAIAGKNLRL
AMDIELQLLG EKMMKGKVGS IVAIDPQTGG ILAMVSGPTF DPNLLSGSYR AKNLGRLLTD
TVSPMFNRAI SASYPPGSTF KPITGLIALD EGTVGPEFGF DCRGGYGNCG RFSKCLHSNV
GHASNMRNAL ANSCNAYFMH LYRLCVDNKK WGNTGAGQAK FVSYLNDMGL GRRLGVDIPN
EKSGDVPDTA RMNRRYSGLW NSCSEMYVGM GQGLLGLTPL QMANAMCIIA NRGFYFVPHF
VESIDDDHSG MLKKYKEKHR VANISDDAFS SVVLGLEDVV TKGTAKGVQI EGVAVCGKTG
TAENKARING QTVQLKDHSL FVGFAPKDNP KIVIAVIVEN SGFSTTYAVP IASILMEKYL
TDSISPKRRL ALDKMIEANT ISPEMKAKSK LDSLNSVSYM ALAGDELLRK IIAK
//
