ID A0A0F4RFL6_9RHOB Unreviewed; 646 AA.
AC A0A0F4RFL6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KJZ18345.1};
GN ORFNames=TW80_15595 {ECO:0000313|EMBL:KJZ18345.1};
OS Loktanella sp. S4079.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ18345.1, ECO:0000313|Proteomes:UP000033741};
RN [1] {ECO:0000313|EMBL:KJZ18345.1, ECO:0000313|Proteomes:UP000033741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4079 {ECO:0000313|EMBL:KJZ18345.1,
RC ECO:0000313|Proteomes:UP000033741};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ18345.1}.
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; JXYE01000007; KJZ18345.1; -; Genomic_DNA.
DR RefSeq; WP_045998374.1; NZ_JXYE01000007.1.
DR AlphaFoldDB; A0A0F4RFL6; -.
DR STRING; 579483.TW80_15595; -.
DR PATRIC; fig|579483.3.peg.3207; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000033741; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT DOMAIN 63..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 646 AA; 70939 MW; A215BB154CD4EF68 CRC64;
MKRPPKDVIE SARTISRRAL VLGASQVAIM AVLGWRMRSM QVEHADEFRL LAEENRINIR
LLPPSRGLIF DRNGEAIADN EQNYRVVMVR EDAGDVGEVL AKLTQIVDIT PEQLSRAMEE
MQRRSPFVPV TIAERLSWED VAKINLNTPA LPGIQAEVGQ SRVYPWGADL AHVVGYVGPV
SDYDLSRIDD QDPLLQIPKF QIGKTGAENK LEHTLRGSAG HRRIEVNAVG RVMRELDRQE
GEAGKDVQLT IDNRLQTYVQ ARLDGESAGV VVIDLEHGDL RAIASAPSFD PNLFVRGISV
KDWTGLNEDK YRPLAAKAVQ GTYPPGSTFK MITALAAMED GVVAADETVY CPGYTDVYGI
RFHCWKSGGH GNINLHDSLK QSCDCYYYEI AQRVGIDKMA AMARKLGLGI RHDLPLSAVA
SGLAPDKEWK STVRGEDWRI GDTVNASIGQ GYVLASPLQL AVMTARIATG HEITPRLVRL
VDGVEQPSGR GESLGLNENT LRRIRASMVD VCNNRRGTAY GSRIIADEYK MAGKSGTSQV
RRITAEERAA GVTRNEDLPW ERRDHALFVS YAPLDNPRYA VAVIVEHGGG GSSAAAPIAR
DVILQAQYGG TPPLEAYPES ARSKIAEQQR RIETRIPAGA KAQSRA
//