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Database: UniProt
Entry: E2ZBV2_9FIRM
LinkDB: E2ZBV2_9FIRM
Original site: E2ZBV2_9FIRM 
ID   E2ZBV2_9FIRM            Unreviewed;       672 AA.
AC   E2ZBV2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Penicillin-binding protein, transpeptidase domain protein {ECO:0000313|EMBL:EFQ04330.1};
GN   ORFNames=HMPREF9429_00934 {ECO:0000313|EMBL:EFQ04330.1};
OS   Megasphaera micronuciformis F0359.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ04330.1, ECO:0000313|Proteomes:UP000003195};
RN   [1] {ECO:0000313|EMBL:EFQ04330.1, ECO:0000313|Proteomes:UP000003195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0359 {ECO:0000313|EMBL:EFQ04330.1,
RC   ECO:0000313|Proteomes:UP000003195};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) 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:EFQ04330.1}.
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DR   EMBL; AECS01000036; EFQ04330.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2ZBV2; -.
DR   STRING; 706434.HMPREF9429_00934; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_0_9; -.
DR   Proteomes; UP000003195; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003195};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          613..672
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   672 AA;  72954 MW;  1F0C31A0B6103D78 CRC64;
     MDKEQLQQKK EQKKDMKMRK RILKCFTGLL IFGLVLTVRL VCLQTVQSAD LTERADAQSE
     ADRKIQSPRG MILDRDGKVL AISEVAKSLY ADPTMMQSDT DGKGKTPAEA AELLAPYLRI
     KQDEIEERLS RDTSFVWLDR TMDDDKYQAL KSVIADKHIK GLRFVDENRR YYPNGTLAAQ
     LIGFVGDNDH GLDGIEMVLD DDIRGDTQKL RLTTDSNNVP IFDSALEKVL PDKEKSVRLT
     IDSTIQYIAE KGLDDIMKNN KPEGAAIIIM NPKTGEILAM ASRPNFDPND YGKANKEAYK
     NRAVVNLYEP GSTFKPLMAS AALDAGTWTE SKTYKDVGYV QVDDRVISNW DDSGMGTVTL
     KEILKFSINT GMVAIGLNTG GKILTSYAEK YGFGKQTGIE LPGEGEGILF NPDEMSNINT
     ATMAIGQGIA VTPLQMVQAF GAVANHGTMM KPFVIKEIDN PDGSVFKKTE PQEVGQPISA
     EVSRIISTIM ADEINSGGGL NAKIDGYNFC GKTGTAQRLN SEGTGYAEGQ YIGSFVGFGP
     LEDPEYVVLI VVDNPSGVYY GAQVAAPIFK MMMTDIVRIK GIRPASAAAA NATVLKSLPA
     AASRAPLPPV DVTGDTVLLP SFIGYDSREV NEWLNAAGLG FIPNGTGLAT YQVPAAGTYV
     DAGSNVTVSF SR
//
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