ID A0A0F5R1B0_9BACL Unreviewed; 770 AA.
AC A0A0F5R1B0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Stage V sporulation protein D {ECO:0000313|EMBL:KKC47012.1};
GN ORFNames=VE23_07445 {ECO:0000313|EMBL:KKC47012.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC47012.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC47012.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC47012.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-2015) 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:KKC47012.1}.
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DR EMBL; JZEJ01000001; KKC47012.1; -; Genomic_DNA.
DR RefSeq; WP_049867675.1; NZ_JZEJ01000001.1.
DR AlphaFoldDB; A0A0F5R1B0; -.
DR PATRIC; fig|665792.3.peg.1663; -.
DR OrthoDB; 9804124at2; -.
DR Proteomes; UP000036611; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR CDD; cd06576; PASTA_Pbp2x-like_1; 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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000036611};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 601..661
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 719..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 82019 MW; 95AB68E608734333 CRC64;
MDTVKRIKLR TLFVGGLITL LFLVLFTRIF WVQVVKADFW LGEAKKIWAA SDTIPAERGS
ITDRNGNLLA MNIPAYTVVV NPKVIQELGI EDQVADGLSK ILGKPKADIV KQVSFRNAKG
EYSQYRELRP EGLNIEKKKS DEVAKLSAQI KKDLEEKRGK KISGSDMGIT LIKGSKRFYP
NNTLAAHLLG FVNKQGDPVI GLEADFNDVL KGTDGKIVYE KDGNRVQVDN GTAKLVPAVN
GKNIKLTIDN EIQHYVQDAI QEAYDLYKPQ SITAIVADPN SMEVLGMANL PTFNPNSYSS
SNPINFNNLA VGGTYEPGST FKIVTLAGAV QEKMFNPNEE YMSGRISVPG QDVYDIKRSG
WGPITYLEGL KRSSNVAFVH LGMERLGKEK LTDYIRNFGF GTKTGIEIKQ EVRGSLNIQG
KSDVARASFG QGPVSVTPIQ QVAAVAAVAN GGKLLKPHIV KEIDDPATDK KTETRTEQVR
QVVTAETSKL TSGFLEQVVS DSKIGTGRNA AIPGYRVAGK TGTAQKIVNG TYSKDKYVVS
FIGYAPVSNP RFVVYVIVDS PSVPDPGGGK IAAPVFKKIV TQSLRYMGVK PDASVPPSQD
KKQPLTVPDL TGLTLAKAQQ ELKARGLASK AVGKGASVLK QMPAAGTIVS DSQSVYLVTE
EENKLQLPSL AGSSLREALQ LCSSVGRKCV TEGEGYVISQ MEAKLNGEPV VKLILKPPAG
EEASDASAAD AAAAGGSASG SKQDGGTDAA GGQPDDSSGG GGSAPPAGGG
//