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Database: UniProt
Entry: A0A0F4RFL6_9RHOB
LinkDB: A0A0F4RFL6_9RHOB
Original site: A0A0F4RFL6_9RHOB 
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}.
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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
//
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