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Database: UniProt
Entry: K2H842_9BACI
LinkDB: K2H842_9BACI
Original site: K2H842_9BACI 
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
//
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