ID N1WKN0_9LEPT Unreviewed; 649 AA.
AC N1WKN0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:EMY76378.1};
GN Name=mrdA {ECO:0000313|EMBL:EMY76378.1};
GN ORFNames=LEP1GSC060_1668 {ECO:0000313|EMBL:EMY76378.1};
OS Leptospira weilii serovar Ranarum str. ICFT.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY76378.1, ECO:0000313|Proteomes:UP000012313};
RN [1] {ECO:0000313|EMBL:EMY76378.1, ECO:0000313|Proteomes:UP000012313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICFT {ECO:0000313|EMBL:EMY76378.1,
RC ECO:0000313|Proteomes:UP000012313};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAR-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:EMY76378.1}.
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DR EMBL; AOHC02000052; EMY76378.1; -; Genomic_DNA.
DR RefSeq; WP_003009945.1; NZ_AOHC02000052.1.
DR AlphaFoldDB; N1WKN0; -.
DR STRING; 1218598.LEP1GSC060_1668; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000012313; 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..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..616
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 627..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 71035 MW; 9DE083207823D0B3 CRC64;
MFGGAQSASE YRLEKSFRFR LYTFSGLVVF TLAAFIFQLF NLQIFNGTDN ALKAEKFVRK
SEILPAARGQ MFDRNFLTPE TSMALVSNYS SLDAVLNTSL FKYDPGATKA FIQEFARTLS
IPISYYQDEL IEPRFSRNLK AKKPIVLLEG ITTAQQERIS VFDNISKYII LLPSPRRIYK
MGPALAHVTG YIGKPTRGDL VSGEIKSYQF LGKSGLELEY DSELRGVDGF RIQKRSSEGN
IEEERVVEHS SPGNNLVLTI DKDIQIAAHK ALKGTRGTAI AIKVSTGEIL AMASNPSYDP
NILSGKNKAD RTAHFNRVKD NGGFLNLAIQ SKFPPASTYK TLVALAALES QHKIGYTPET
TFSCNGSFVL KSTFAGVPDQ VFNCWEKGGH GTNDLAHALQ KSCSVYFYNL GYKLGSDAIL
NYSRLFGLES QSKVDLPGEI TGFIPSSAWK KRTYGTKWFD GDTINLSIGQ GFISSTPMGM
ALFYMGILNR GQIYQPYLVS EIRDPVDNSI INRTAPQILR DIPINQSSVD AIKEGLKLVV
KSGTAAYVLN KPYLPDIAGK TGTAQTRRRG ASGSNHAWFV GYAPASAPAS EQVLVVVFVE
YGVGGAAGAA PVARDMFHAA FPPGTFKKSQ DITPPSLPST GQEGSLETR
//