ID K2H842_9BACI Unreviewed; 713 AA.
AC K2H842;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=MJ3_06913 {ECO:0000313|EMBL:EKE31850.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE31850.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE31850.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE31850.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
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 -!- 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:EKE31850.1}.
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DR EMBL; AMPQ01000007; EKE31850.1; -; Genomic_DNA.
DR RefSeq; WP_008589747.1; NZ_JAFBFF010000006.1.
DR AlphaFoldDB; K2H842; -.
DR STRING; 1230341.AAV35_007485; -.
DR KEGG; sje:AAV35_007485; -.
DR PATRIC; fig|1230341.3.peg.1431; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9804124at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000011746; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd06575; PASTA_Pbp2x-like_2; 1.
DR Gene3D; 2.20.70.70; -; 1.
DR Gene3D; 3.30.70.2110; -; 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; 2.
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:UP000011746};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 652..709
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
SQ SEQUENCE 713 AA; 78934 MW; D1FE8E5130EAB704 CRC64;
MKHRNTSRGA SLLLIIFSIA FLLIAGRFLY IQTTGSVQGV DLEKWAEKKR TSSYTLPSER
GEIYGKNGMV LAYDRPTYRL QAIVDPSYSE NLPEPKHVTS PEDVGEVVSG HLNLEKEEVV
KRIKEAKKSG KFQVEFGSKG RDIAKDDKEV IEEALKEKSV SGVTFAEETE RYYPNGTFAS
HVLGFAKSTD EGVEGVTGVE KSMEKYLEGE DGKISYKRDK YGTELLNPEE VLHPPEDGED
VYLTIDQKIQ TFLEDALTEV EEKYEPSKIM AGVMDPDTGE ILAMGNRPAY DPNDRSNVEN
WYNDMIAYPF EVGSTMKMFT WASAMEAGVY DGSEKFKSGA YSVDGSTISD HNRTGWGSIS
YDEGLIRSSN VAAAKLGYEK LGPDRFEKYI SKFNLNAKTG IDLPGEKTGT ILNDRPIETV
TTAYGQGSTM TPLQLLTAAT AIANDGKMMK PYVFDSIREA NSSDKITENE SSVLGKPISE
ETAEKMRKLL RKVVSDEKGT GKPFALEDFK VAGKTGTANI SEGGYLSGRN NYTFSFLGMA
PADDPELVMY VAVRQPQLEN SEVGSDAVSH VFKTVMQNSL HYLNISPEQK EKSKVKMMDI
PDLQGASVEK AKTALSGFKE VTVIGEGARV EAVLPESEKD VVSSEHIFVI TGQPEMPDME
GWSQREAQRL TDYFDIPFEM KGNGYIKEQS IEEGSDLTKV KQVEVQLEPP EEG
//