ID A0A074JWR9_9RHOB Unreviewed; 580 AA.
AC A0A074JWR9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=DT23_02335 {ECO:0000313|EMBL:KEO60345.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO60345.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO60345.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO60345.1,
RC ECO:0000313|Proteomes:UP000027471};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(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:KEO60345.1}.
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DR EMBL; AUNB01000018; KEO60345.1; -; Genomic_DNA.
DR RefSeq; WP_038129456.1; NZ_AUNB01000018.1.
DR AlphaFoldDB; A0A074JWR9; -.
DR STRING; 1353528.DT23_02335; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000027471; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000027471}.
FT DOMAIN 62..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 269..580
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 580
FT /evidence="ECO:0000313|EMBL:KEO60345.1"
SQ SEQUENCE 580 AA; 64368 MW; 11C12B3634DB57D5 CRC64;
MRRSPKETQE STRRITRRGL MLGGAQLAVV AVLAARMRKM QVEDASQYRL LAEGNSVKIR
LIPPARGLIY DRNGVLLAGN EQNYRVTITR EDSDDVDATL AELRRLVPIT DSDAADILHD
IRRRPPTTPV TVADRLTWDE FSRVAVNSPS LPGVNPDVGL SRLYPRHDDF AHVIGYVGPV
SDYDLSKMDD PDPLLMIPKF QLGKTGIEAK EEDVLRGEAG QRRIEVNSAG REMRELSREP
GKPGENLQLT VDYRLQNYAL QRLEEESAAT VLIDVTNGDV LACASAPSFD PNMFVRGISV
AQYKTLTQDD HRPLADKSVQ GLYPPGSTYK MVTALAALEA GLVKPNETVW CPGYVEIAGR
RFHCWKRAGH GHVDMTKSME QSCDVYYYEM SQRVGIDKMS EMANRLGLGV RPDLPMSAVK
EGVAPTKEWK KERYGKDWLI GDTANAAIGQ GYVLASPMHL AIMTARIASG KKVEPRLIRT
RDGIEQPVRV SDDLGIAKAH LDDVRKGMTA VVNSSRGTGR GSRIAMAEWK MAGKSGTSQV
RNISKAERAR GVIRNDQLPW DRRDHALFVA FAPIDNPRYA
//