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Database: UniProt
Entry: A0A1M7E9I6_9GAMM
LinkDB: A0A1M7E9I6_9GAMM
Original site: A0A1M7E9I6_9GAMM 
ID   A0A1M7E9I6_9GAMM        Unreviewed;       402 AA.
AC   A0A1M7E9I6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=L,D-transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SHL88432.1};
GN   ORFNames=SAMN05878437_0067 {ECO:0000313|EMBL:SHL88432.1};
OS   Halomonas subglaciescola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=29571 {ECO:0000313|EMBL:SHL88432.1, ECO:0000313|Proteomes:UP000190911};
RN   [1] {ECO:0000313|EMBL:SHL88432.1, ECO:0000313|Proteomes:UP000190911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 12 {ECO:0000313|EMBL:SHL88432.1,
RC   ECO:0000313|Proteomes:UP000190911};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
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DR   EMBL; LT670847; SHL88432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7E9I6; -.
DR   STRING; 29571.SAMN05878437_0067; -.
DR   InParanoid; A0A1M7E9I6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000190911; Chromosome i.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00118; LysM; 1.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF24; L,D-TRANSPEPTIDASE ERFK_SRFK-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS51782; LYSM; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190911};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..402
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009925371"
FT   DOMAIN          108..153
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          67..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  43326 MW;  DE21BBF0B991B424 CRC64;
     MTSQKTDHRR LRKAPAVTLL AAAIGAAWLT LPATASAVSL KDAAAEETGN ISAAALSSVK
     TLMTAQQEQA ASKKQQTSRQ PAPAATPNDL PRGQFHLPDE GDVIGKHYTI VVQDQEQTLV
     DIARQHNIGY EEIRMANPGV SLWVPGKGTE VTIPSRYLLP DAPRKGIIIN LSELRLYYYP
     ADKPGIVETY PVSVGREEFA TPVGVTRTTI KVKDPAWAPP ASMRREAAER GDPAPEIVPA
     GPDNPLGRHA ILLDLPSYLI HGTNRPEGVG MRVSRGCIRM YPEDIKSLYE RLPGNTRVNL
     IDAPFKAGWD ADGSLLVQSF PQLEENSVDV EPLLDALKMV DAQTKDGVEI DYARVKQAIG
     DSDASIIALT GPQASPTPDA AKSRNTAELL EEIQLESASA GE
//
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