SP5D_BACSU
ID SP5D_BACSU Reviewed; 646 AA.
AC Q03524;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Stage V sporulation protein D;
DE EC=3.4.16.4 {ECO:0000305};
DE AltName: Full=Sporulation-specific penicillin-binding protein;
GN Name=spoVD; OrderedLocusNames=BSU15170;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND PENICILLIN-BINDING.
RC STRAIN=168;
RX PubMed=8289242; DOI=10.1016/s0022-2836(05)80027-0;
RA Daniel R.A., Drake S., Buchanan C.E., Scholle R., Errington J.;
RT "The Bacillus subtilis spoVD gene encodes a mother-cell-specific
RT penicillin-binding protein required for spore morphogenesis.";
RL J. Mol. Biol. 235:209-220(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 540-549.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC STRAIN=168;
RX PubMed=8244929; DOI=10.1128/jb.175.23.7604-7616.1993;
RA Yanouri A., Daniel R.A., Errington J., Buchanan C.E.;
RT "Cloning and sequencing of the cell division gene pbpB, which encodes
RT penicillin-binding protein 2B in Bacillus subtilis.";
RL J. Bacteriol. 175:7604-7616(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-646.
RC STRAIN=168;
RX PubMed=8436954; DOI=10.1099/00221287-139-2-361;
RA Daniel R.A., Errington J.;
RT "DNA sequence of the murE-murD region of Bacillus subtilis 168.";
RL J. Gen. Microbiol. 139:361-370(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=168;
RX PubMed=8636036; DOI=10.1128/jb.178.8.2343-2350.1996;
RA Daniel R.A., Williams A.M., Errington J.;
RT "A complex four-gene operon containing essential cell division gene pbpB in
RT Bacillus subtilis.";
RL J. Bacteriol. 178:2343-2350(1996).
CC -!- FUNCTION: Penicillin-binding protein with an unknown catalytic
CC activity. May have a specialized role in the morphogenesis of spore
CC cortex, which is a modified form of peptidoglycan. Spore cortex
CC formation is determined primarily by the mother cell.
CC {ECO:0000269|PubMed:8289242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000305};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8289242};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed during sporulation; strong expression
CC 60-150 minutes after sporulation onset, falls to background expression
CC by 240 minutes. Found only in mother cells.
CC {ECO:0000269|PubMed:8289242}.
CC -!- DISRUPTION PHENOTYPE: Asporogeneous; spore development starts but does
CC not develop the spore cortex. {ECO:0000269|PubMed:8289242}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR EMBL; Z25865; CAA81085.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13390.2; -; Genomic_DNA.
DR EMBL; L09703; AAC36838.1; -; Unassigned_DNA.
DR EMBL; Z15056; CAA78766.1; -; Genomic_DNA.
DR EMBL; Z68230; CAA92528.1; -; Genomic_DNA.
DR PIR; S49570; S49570.
DR RefSeq; NP_389400.2; NC_000964.3.
DR RefSeq; WP_003245048.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q03524; -.
DR SMR; Q03524; -.
DR STRING; 224308.BSU15170; -.
DR PaxDb; Q03524; -.
DR PRIDE; Q03524; -.
DR EnsemblBacteria; CAB13390; CAB13390; BSU_15170.
DR GeneID; 936661; -.
DR KEGG; bsu:BSU15170; -.
DR PATRIC; fig|224308.179.peg.1653; -.
DR eggNOG; COG0768; Bacteria.
DR InParanoid; Q03524; -.
DR OMA; SCDTYYY; -.
DR PhylomeDB; Q03524; -.
DR BioCyc; BSUB:BSU15170-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 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 Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR02214; spoVD_pbp; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Protease; Reference proteome; Sporulation.
FT CHAIN 1..646
FT /note="Stage V sporulation protein D"
FT /id="PRO_0000195466"
FT DOMAIN 580..638
FT /note="PASTA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT ACT_SITE 294
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
FT CONFLICT 540..549
FT /note="TIQFGGTVAA -> AFSLAERWQ (in Ref. 1; CAA81085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 71118 MW; 7F576F8DF2E1085C CRC64;
MRVSNVTVRK RLLFVLLFGV IVFLIIDTRL GYVQFVMGEK LTSLAKDSWS RNLPFEPERG
EILDRNGVKL ATNKSAPTVF VVPRQVQNPM KTSKQLAAVL NMSEEKVYKH VTKKASIEKI
TPEGRKISNE KAKEIKALDL KGVYVAEDSI RHYPFGSFLS HVLGFAGIDN QGLLGLEAYY
DDDLKGEKGS VKFYTDAKGK KMPDEADDYT PPKDGLDMKL TVDSKVQTIM ERELDNAEAK
YHPDGMIAVA MNPKNGEILG MSSRPDFDPA DYQSVDPSVY NRNLPVWSTY EPGSTFKIIT
LAAALEEQKV NLKRDQFYDK GHAEVDGARL RCWKRGGHGL QTYLEVVQNS CNPGFVELGE
RLGKEKLFKY IKDFGFGQKT GIDLQGEGTG ILFPLERVGP VEQATTAFGQ GVSVTPIQQV
AAVSAAVNGG TLYTPYIAKE WIDPVTKKTV KKQSPIAKKQ VISEETSKQI RYALESVVAE
GTGRNAFVEG YRVGGKTGTA QKVKDGKYLE NNHIVSFIGF APADDPSLVV YVAVDNPKGT
IQFGGTVAAP IVGNIMRDSL PELGVKPRKN QIEKKYQWND TKTIEVPNVV GMSVSDLESL
LVNLNVDASG KGSKIVKQSP AAGTKVKEGS KIRVYLTEED EKEAAD
