ID A0A098M6B7_9BACL Unreviewed; 641 AA.
AC A0A098M6B7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:KGE18114.1};
GN ORFNames=PWYN_26640 {ECO:0000313|EMBL:KGE18114.1};
OS Paenibacillus wynnii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=268407 {ECO:0000313|EMBL:KGE18114.1, ECO:0000313|Proteomes:UP000029734};
RN [1] {ECO:0000313|EMBL:KGE18114.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18114.1,
RC ECO:0000313|Proteomes:UP000029734};
RA den Bakker H.C.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE18114.1, ECO:0000313|Proteomes:UP000029734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18334 {ECO:0000313|EMBL:KGE18114.1,
RC ECO:0000313|Proteomes:UP000029734};
RA Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGE18114.1}.
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DR EMBL; JQCR01000003; KGE18114.1; -; Genomic_DNA.
DR RefSeq; WP_036657876.1; NZ_JQCR01000003.1.
DR AlphaFoldDB; A0A098M6B7; -.
DR STRING; 268407.PWYN_26640; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000029734; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR CDD; cd06573; PASTA; 1.
DR Gene3D; 3.30.10.20; -; 1.
DR Gene3D; 3.30.450.330; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR011927; SpoVD_pbp.
DR NCBIfam; TIGR02214; spoVD_pbp; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF19; STAGE V SPORULATION PROTEIN D; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000029734}.
FT DOMAIN 579..638
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 641 AA; 69602 MW; B06F3340197761CA CRC64;
MKVSKVVTRR RMLYTLLSLA VLFAALVVRL AYVQLSEGNE LSAKAEDSWR RNIPFTAKRG
EILDREGIAL SYNISSPTVI AIPVQVKEKQ KTAQQLAPLL GMTEDKLTAL LSKRESTVKL
QPGGRKITME LAGKIRDLQL PGIVVAEDNK RYYPYGDLAA HILGFTGIDN QGITGVERVY
DKLLQGIEGN ISYLSDAGGR LMPGSSEKYS APLDGLSLQL TIDKQIQSIM ERELDQAMVK
YQAQGSWAIA MNPKNGEILA MASRPGYEPG NYKEYNTETY NRNLPIWMTY EPGSTFKIIT
LAAALQEGKV DLQNDLFFDP GFIEVGGARL RCWKKGGHGS ETFMQVVENS CNPGFVALGQ
RLGKETLFKY IRNFGFGTKT GIDLNGESNG ILFKPAQVGP VELATTAFGQ GVSVTPIQQI
AAVSAAINGG NLYKPHVAKA WINPETGKTV SVVSPELVKQ VISAETSKKV REALESVVAK
GTGRPAFIDG YRVGGKTGTA QKVINGHYST TEHIVSFIGF APADDPQIVV YTAVDNPKGI
QFGGVVAAPI VQNILEDSLH YMKVPERSDQ LPKTYKLGEV PIVTVPDLTG ASVQDIYEDL
NMNFSLARSG SGSVVINQAP KAGTRVEQGS TIRIYMGSPS E
//
