ID A0A0V8JFN4_9BACI Unreviewed; 671 AA.
AC A0A0V8JFN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=AS030_09810 {ECO:0000313|EMBL:KSU85770.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU85770.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU85770.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU85770.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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}.
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:KSU85770.1}.
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DR EMBL; LNQN01000001; KSU85770.1; -; Genomic_DNA.
DR RefSeq; WP_061971089.1; NZ_KQ758617.1.
DR AlphaFoldDB; A0A0V8JFN4; -.
DR OrthoDB; 9770103at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000054099; Unassembled WGS sequence.
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:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000054099}.
FT DOMAIN 59..288
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 339..644
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 671 AA; 75075 MW; 45A916E1704948B9 CRC64;
MTKETKKKNH VPIRLNALFL AVFFLFSILI FRLGYVQIVQ GEEYQRSADK KENVTARLDA
PRGKMMDTEN RVAVDNKPVY SITYTRTQKT SAEDREAIAE KLAGYIKKDT KNVTERDKKD
YFIFLHQKEV ESRISPAEKK QLNDDQYYKL MLDRITKKDL DSFTPHQIEV LAIKREMDSG
YALTPQRIKI GASQKEIATI SEHLSDLPGI DIKPDAKRDY PYGDTFKALF GQVKQIPSSK
MDFYLSRGNE RNDLVGTSFL EEQYESLLRG KKSSVRYVTD KAGNPVGEPV EVEGSRGKDL
TLTVNMELQQ KVEDVIEKAM KKAKSGGSAY ANRDLTEAYV VMMNPENGEI LSMAGKKYDT
KTGQYKNAPF GTVYNSFEMG SAVKGATVLT GLQKGAITPA THFYDAPLVF GDGRKMKSAH
SGLGSIGPVE ALEASSNVYM WHVAMKLAGY DYSHKRFIDH HVDEAFRVLR DSYSQFGLGV
PTGIDLPSEA TGYNTGMSDQ LAQAMFFAIG QFDTYTPLQM AQYVSTIANN GYRMQPHLLK
EVREPSTQPG KLGKLDYKFE PHVMNKIEMK QEYLDVVHQG FRQVMVGSHG TAAAYFKNKS
YQPAGKTGTA QVDVKSGLNN KTLVGYAPYD NPEVSFAVVV PKVREGSINL EIGSGALDAY
FKLKKDGNKT K
//
