ID A0A1A9GL42_9ACTN Unreviewed; 715 AA.
AC A0A1A9GL42;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:ANH38816.1};
GN Name=spoVD {ECO:0000313|EMBL:ANH38816.1};
GN ORFNames=I601_2398 {ECO:0000313|EMBL:ANH38816.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH38816.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH38816.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH38816.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-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}.
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DR EMBL; CP015079; ANH38816.1; -; Genomic_DNA.
DR RefSeq; WP_068109844.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GL42; -.
DR STRING; 1300347.I601_2398; -.
DR KEGG; ndk:I601_2398; -.
DR PATRIC; fig|1300347.3.peg.2390; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000077868; Chromosome.
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:UP000077868};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..253
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 305..668
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 686..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 77145 MW; 4A97FF3976E84C7C CRC64;
MRAPTRGEEA AGTRRSRLRI LVIQALVLSL FATLLVRLYY IQVVTGEEYT AQAASQSVRD
IVVQPQRGLI VDDMGRPLVT NRTAWVVSVD RTLLGKMGGR DRREVLNRVA VVTGAGRSEV
EKRLVTCGDA GSVSGTCWNG SPYQPVPVAT DVERGVALKI LEQPEDYPGV LAEQQTVRAY
PRPYGVNLAH VLGYLSPITE DELDQADSDG DASVNGASSV GRAGVEKQYD AWLRGMPGYQ
SVAVDSMGRV LGEDSQTQAR PGDTLVTSID ARVQSVVEKQ LAETIKTARA TTDTVTGRRY
AADSGAAIVL EADTGRVVAM ASQPTYDPEV WVGGISDKEL AHLYSEAAGT PLLGRATQGQ
FAPGSTWKPF MTAGALSNGY GTDTMLNCSS ALRVGNRDFK NYESGAYGFI GFAKALEVSC
NTFFYRVGLD YWQRYGSDVS DVDAKDPLVQ EAKDWGFGAE TGIDMPGEAP GRIADRQWKR
DYYESMKDYY CGISEKPQDA ETSDFVYRFS REFCVEGFAY RAGDAVNFAI GQGDTIVTPL
QLARAYGAIA NGGTLYEPRI AKAVVGPDGK VLRRIDPEVQ GEVDLPAKTF GYIDEALAGV
TRQGTMSWRM IGFPLEEVPI RSKTGSAEVY GKQSTSWVAS YSEDYVVVMM VSQGGTGSGT
SGPAIRTIWE TLYGVDGEQV RPAKAAIPGT TPPTQLPTFT RDGSVLPPAR AKGDS
//
