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Database: UniProt
Entry: A0A0S6VWY5_9BACT
LinkDB: A0A0S6VWY5_9BACT
Original site: A0A0S6VWY5_9BACT 
ID   A0A0S6VWY5_9BACT        Unreviewed;       630 AA.
AC   A0A0S6VWY5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=MrdA protein {ECO:0000313|EMBL:GAK50479.1};
GN   ORFNames=U14_01710 {ECO:0000313|EMBL:GAK50479.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50479.1};
RN   [1] {ECO:0000313|EMBL:GAK50479.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; DF820456; GAK50479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S6VWY5; -.
DR   STRING; 1499966.U14_01710; -.
DR   HOGENOM; CLU_009289_1_2_0; -.
DR   Proteomes; UP000030700; 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, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..239
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          271..604
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   630 AA;  69894 MW;  8AEEA7E9F484D333 CRC64;
     MHQQFHQRSS IIVKFRLGVY IGVVLLLFAV LVGRLWYLQI IQGEQFLKKS EENRIRLLRI
     RAPRGIISDA DGFALVRNRP SFNVYLIRED VPLKKGGKTQ DFETIAAHLD ELLPISKDEI
     LDKINKSTRP KFEPTLIFRD ASLKTVAYLE EHKIELPGVM VDVEPLRYSI YDSGVCHVVG
     YLGEINEKEL KDTLNNPDAV QGDLVGKSGI EQTFNLYLSG KPGGKQIEVN AHGRELETIS
     QKNPMPGNNI MLTLNLHIQL IAEEALGDKI GAIVAVDPRN GHILAMVSHP GFNPNFFAGG
     ISSDNWKSLV KNPDKPLQNK AIQSHYAPGS TFKPMIGSAL LQNRIVSSTS ASFCGGQFSA
     ANTTKRCWKT GGHGYLNIKQ AIEQSCNVFF YRNGLELGID ELARYAMSFG LGAKSGIELP
     NEVPGLIPTR EWKQETIGDK WYPTETMDAA IGQGFVAVTP LQLAMMTSVI ANGGTLYKPQ
     IVKKIVRPNG EILKEYEPTV VRKVPIDEKH FKTIREGMWM VVNGTKGTAR GSQLKTFQFA
     GKTGTAQVVK LQRGSQEGLP EKFRDHGWFI CFAPAEKPEI AMAIIVEHGM GGAKAAAPVA
     KYIFERLFTP QELLVEQPVM EPTELDTLED
//
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