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Database: UniProt
Entry: A0A074JWR9_9RHOB
LinkDB: A0A074JWR9_9RHOB
Original site: A0A074JWR9_9RHOB 
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
//
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