ID A0A1U7MAC2_9FIRM Unreviewed; 604 AA.
AC A0A1U7MAC2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:OLS54386.1};
GN Name=spoVD_5 {ECO:0000313|EMBL:OLS54386.1};
GN ORFNames=SPSPH_44680 {ECO:0000313|EMBL:OLS54386.1};
OS Sporomusa sphaeroides DSM 2875.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS54386.1, ECO:0000313|Proteomes:UP000186950};
RN [1] {ECO:0000313|EMBL:OLS54386.1, ECO:0000313|Proteomes:UP000186950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS54386.1,
RC ECO:0000313|Proteomes:UP000186950};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:OLS54386.1}.
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DR EMBL; LSLJ01000008; OLS54386.1; -; Genomic_DNA.
DR RefSeq; WP_075758042.1; NZ_LSLJ01000008.1.
DR AlphaFoldDB; A0A1U7MAC2; -.
DR STRING; 1337886.SPSPH_44680; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000186950; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186950};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..220
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 266..587
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 202..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65530 MW; 3D5AF39E294E961E CRC64;
MWIEQIRRLK IVGLVVVGIV SLLVLRLVWL QLLQGAHYKK NAEQNRTRQI SVQAPRGVIY
DRNGEILVSS RPSFAVSIVP HEYTNPQEAT PLLASITGVA VEEINQLLAD SIDFPYTPVR
IQRNADDVMI ARIQERQYYL PGVVLEAIPV RQYVYEELAS HVLGFVGRIS QEEYARNKEQ
GYHPADLVGK DGLEREWEEV LRGTDGSRQS EVNASGEEVR PLGNRPSVTG RGLVLTLDAN
LQKAAEEALA AQVAASRTIG EPAKGGSVVV LDVNTGGVLV MASNPPFNPN LFAGGISSKA
WNELIANPDH PLNNRAIQNA YPPGSVFKIV TAAAALEMNL TTPQEIFDDR GVYVLNGWRF
YGWNVKGLGK LNIVDGLSLS SDPVFYELGR RLGADNLAAY ALTFGLGKAT GIKLAGEVKG
IVPYIEWKQA NYGEPWYPGE TLIAAIGQGY YLATPLQQAL LTMAVANGGI VYKPRLVDQV
LTPEGSLAAS LPPEVLWTIY LRPEVWDTVR QGLIAVTTRG TGAAAFKDFP QTIAGKSGSA
ETGRGTTHSW FACYAPAEKP EIAMAVLVEE GGDASVAAVP VTRRVLEAYF GIPNKQLPPA
PTTD
//
