ID A0A0Q9LSA5_9MICO Unreviewed; 634 AA.
AC A0A0Q9LSA5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Penicillin-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG70_03655 {ECO:0000313|EMBL:KRE56252.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE56252.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE56252.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE56252.1,
RC ECO:0000313|Proteomes:UP000051855};
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 -!- 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:KRE56252.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMSC01000006; KRE56252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9LSA5; -.
DR STRING; 1736397.ASG70_03655; -.
DR Proteomes; UP000051855; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; 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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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}.
FT DOMAIN 155..309
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 354..628
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 634 AA; 64499 MW; B3C52CAE5D7A3161 CRC64;
MGSVAAVVVV AAAAGGGLWW QHSEAAKTSD REAAAAVDAF AAGWAQRSFP KSGARFAGTT
AQAVQDSFTK ATQGLGSGPV KVEPGTVNRK GDRATSTVAV TWTLPGGVPW SYDVPLTAKP
AGSGDAWAVS LPASATAWAP GLGSGATLSA SRTWGQRGDL LDRDGQPLMP VGKVYPVQID
PSRATAATVR QLEKVVDEPA GSLVAKLEAA TKSGSKAPIA VITYRESDFQ QRKAALDGLK
GIIYPVREQP LARTRTFGQP LLGSYGPVNA EQVSASKGRY VAGDYAGVSG LQGRYDAELA
GTPGVQVTSS AKPDSPLFSK DAVDGKDVQT TLSPDAQTAA ESAVARTGSV PSALVAVDVR
TGDVLASANS PALGFDRALT GQYPPGSSFK IVSTYALLTG GKVTPTTSVD CPEKFVVDGR
SYKNYEGESF GKPDFATDFA HSCNTAFVKL STDLGDSDLS KAADALGLTG WAKGVGVGNA
FAASVPTNNG KTDKASAMIG QGRNLTSPLA LATMSASVAR GSAIPPALVT EPAPAGADRT
PRPLDAGAVK ELRALMRQVV TGGTGTVLRD APGGPVSGKT GTAEFGSANP PETHAWFVGY
QGDVAFAALV EKGKSGGTVA APVVKDFLAA LAMK
//
