ID T0Z796_9BACT Unreviewed; 614 AA.
AC T0Z796;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:EQD24944.1};
GN Name=mrdA {ECO:0000313|EMBL:EQD24944.1};
GN ORFNames=D084_Lepto4C00305G0003 {ECO:0000313|EMBL:EQD24944.1};
OS Leptospirillum sp. Group IV 'UBA BS'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD24944.1, ECO:0000313|Proteomes:UP000017751};
RN [1] {ECO:0000313|EMBL:EQD24944.1, ECO:0000313|Proteomes:UP000017751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23645189; DOI=10.1128/AEM.00202-13;
RA Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C.,
RA Hettich R.L., Banfield J.F.;
RT "New group in the Leptospirillum clade: cultivation-independent community
RT genomics, proteomics, and transcriptomics of the new species
RT "Leptospirillum group IV UBA BS".";
RL Appl. Environ. Microbiol. 79:5384-5393(2013).
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:EQD24944.1}.
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DR EMBL; AURA01000305; EQD24944.1; -; Genomic_DNA.
DR AlphaFoldDB; T0Z796; -.
DR PATRIC; fig|1260983.3.peg.743; -.
DR HOGENOM; CLU_009289_1_2_0; -.
DR Proteomes; UP000017751; 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:UP000017751};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..235
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 267..594
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 614 AA; 67604 MW; A019AC259EB8FF6F CRC64;
MASEYRFHKH GILGSPRARL YGLIFVFWLG LAVVVVRLYV VQVIKHRHYL AIARDNVVKV
VPIPPLRGEI TDRNGVVLVR NGPDFAVFEI PAEVRHPRRE LSWLAYDLGI PTEKLRHALS
RLGYVLPPHM PIPLETGLSM AQVGRVNMDL YRLPGFYIQV MPKRIYPPGN VAAHLLGYVG
SFTSADLKGS IYRHLPPGTG IGKSGIEKEY DALLQGSPGL RRQLVDSRGR MIRNLRNDPP
KEGRSLRLTI DMRLQMTAER FLGDRRGAVV ALDPRNGEIL ALASHPAYNS EELSQAMSSS
RWNTLVHATD HPLTDRATQG LYPPGSVFKI VTTLAGLTEH KLDPDMPFRC GGTFRVGSVI
FHDWKRGGHG TLRLHRAIEQ SCDIYFYRLG MTLGPEPIAR MARLFGLGSR TGIDLPAELS
GVVPDREWKR KALHNPWYPG ETPPLAIGQG YLTVTPLEMA RLMGAVAMDG QLSRPHLLLG
EGEKRGGAER SALTGVPVPK KDFDIVRADL RDVVADPHGT GHPVNLPFFS IAGKTGTAQV
VSNRGKNKGL KRPKADSWFV GFGPFENPRI VVAVLIENGG DGGDVAGPVA REVFRMFYIT
RLAGKGTPSP AVSS
//