ID M3H4N2_LEPBO Unreviewed; 648 AA.
AC M3H4N2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:EMG02019.1};
GN Name=mrdA {ECO:0000313|EMBL:EMG02019.1};
GN ORFNames=LEP1GSC123_0202 {ECO:0000313|EMBL:EMG02019.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMG02019.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMG02019.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMG02019.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMG02019.1}.
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DR EMBL; AKWO02000010; EMG02019.1; -; Genomic_DNA.
DR AlphaFoldDB; M3H4N2; -.
DR Proteomes; UP000011783; 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:UP000011783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..244
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 277..615
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 627..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71131 MW; 27F54FA15A022E1D CRC64;
MFGGAQSASE YRLEKSFRLR LYIFSGLVVF TLAAFIFQLF NLQILNGTSN ALKAEKFVRK
SETMPAARGQ MFDRNFLTPE TSMALVSNYS SLDAILNTSL FKYDPASVKA FIQEFARTLS
IPISYYENEL IEPRFSRNLK AKKPIVLLEG ITHAQQERIS AFDNISKYII LLPSPRRIYK
MGPALAHVTG YIGKPTREDL LSGEIKSYQY LGKSGLELEY DSELRGVDGF RIQKRSSEGN
IEEERVVEHS SPGNNLILTI DKDIQIAAHK ALKGSRGTAI AIKVSTGEIL AMVSNPSYDP
NILSGKNKAD RTAHYNRVNS NGGFLNLAIQ SKFPPASTYK TLVALAALES QHKIGYTPET
TFSCNGSFVL KSTFAGVPDQ VFNCWEKGGH GINDLAHALQ KSCSVYFYNL GYKLGSDAIL
NYSRLFGLED KSKVDLPGEI TGFVPSSAWK KRTYGTKWFD GDTINLSIGQ GFISTTPMGM
ALFYMGLLNR GQIYQPYVVS EIRDPVDNSI INRTTPQILR DIPINQSSAE AIKEGLKLVI
KSGTAAYVLN KPFLPDIAGK TGTAQTRRRG SSGSNHAWFV GYAPANAPVS EQVLVVVFVE
YGVGGAAGAA PVAREMFHAA FPPGTFKKSQ DITPSSPSTG QEGTFEAR
//