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Database: UniProt
Entry: A0A0Q7BCH1_9ACTN
LinkDB: A0A0Q7BCH1_9ACTN
Original site: A0A0Q7BCH1_9ACTN 
ID   A0A0Q7BCH1_9ACTN        Unreviewed;       712 AA.
AC   A0A0Q7BCH1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:KQW48427.1};
GN   ORFNames=ASC77_06605 {ECO:0000313|EMBL:KQW48427.1};
OS   Nocardioides sp. Root1257.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW48427.1, ECO:0000313|Proteomes:UP000051939};
RN   [1] {ECO:0000313|EMBL:KQW48427.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW48427.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW48427.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW48427.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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:KQW48427.1}.
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DR   EMBL; LMDV01000008; KQW48427.1; -; Genomic_DNA.
DR   RefSeq; WP_056151123.1; NZ_LMDV01000008.1.
DR   AlphaFoldDB; A0A0Q7BCH1; -.
DR   STRING; 1736439.ASC77_06605; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000051939; 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   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051939};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..249
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          302..669
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   712 AA;  77018 MW;  973B966281CB27B1 CRC64;
     MSPQNQNATQ RTGRLRLLVI QALVFSLFAT LFVRLYYLQV VGGDEYHAQA TSQSVREVVV
     QPQRGLIVDD MGRPLVANRT SWVVSIDRTV LGKLDEHQQK VLLERVAGVV DVPAHRIRKQ
     LVTCGDEGSE PGVCWNGSPY QPVPVAEDVK KSVALRVLEQ PEDFPGVVAE QQSVRAYPQP
     YGINLAHVLG YLSPITEDEL DQAEQDDDTS VNGASSVGRA GIEKEYDRWL RGMPGYKSVA
     VDSMGRVLGD DGEVAGEPGN TLVTSIDAKV QGIVERQLAD TIATARTQYD PVTHKNYVAD
     SGAAVVMEAK TGRIVAMASQ PTYDPSEWVG GISKKQLARL YSAQADNPLL SRATQGQFAP
     GSTWKPFMST GALSDDLGPD TRLGCTSGLQ IGNRWFKNYE SESYGNIGFA EALNVSCDTF
     FYRVGLHFWQ KYGSDPADSK AKDPLAAAAH TFGFGEKTGI DIPGEASGRV GDRVWRASYY
     ASMKDYYCSM DRKGTAKTAF LKLFAHEFCL EGNYFRQGDS ANFTIGQGDT IVTPIQLARA
     YAALSNGGTL YAPRVGKAIV GPDGALVKKI PPKVVGHAKV TRQAIDYVDN ALLGTVRSDG
     AWNGTLAWKF GDFPLDRVHL RGKTGSAEVE GKQSTSWVAT YDKDYVVIMM VTQAGTGSGT
     SGPAVRKIWE ALYGIDGMTV NPKKAAIAGT TPPSALPTFM RDGSILPPKK GD
//
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