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Database: UniProt
Entry: B4SIP6_STRM5
LinkDB: B4SIP6_STRM5
Original site: B4SIP6_STRM5 
ID   B4SIP6_STRM5            Unreviewed;       506 AA.
AC   B4SIP6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ACF51635.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_1931 {ECO:0000313|EMBL:ACF51635.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF51635.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF51635.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF51635.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF51635.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4SIP6; -.
DR   STRING; 391008.Smal_1931; -.
DR   KEGG; smt:Smal_1931; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_480388_0_0_6; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ACF51635.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..506
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002823350"
FT   DOMAIN          263..381
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   506 AA;  55536 MW;  683B2A48F1101571 CRC64;
     MECMNALRCS AFALIIAGLS AGPAAIAQPA HAMIETDPAL DLLLTREAQR MLDAHQFRTS
     RSTQVVVNAS VDLERQRLII RFGPGMLPAE DDHSLEEIEQ YIRSSLEFYA LRSGAGEVQS
     EVLYEGKPYW EHFPIMPAAP AQSSDASTVN SVLVSASHGL VRVHPGLEWE FQRPARNGVQ
     EDLITVGYAE ELQQLMEERG GRVVHRARRN QGDLHPESKR AWSEMSSRYH LRDLLPDRPD
     IWNHFANSTA TDREVSDDIR ARPYYANHLG AAGLFSIHTN ADASGAARGT RVYYHPRKPS
     DQRLADMVLC YMRELITAQE EYADFPVAAA GAAASHGENG FAQMPSVVVE VAFHTNPTDA
     AALLDPAFRT ASMKGVEKGY RLFREGEGCV PLKVEPIQSI ELSAGNSRRV DIVFEGHPRY
     PIDLVTTNVG CPPGWTCTDG KVHIAAPDEK PSQIIMRCEN AGSAPLFWNT QVVDADGVKS
     PPVRHRVQCI RRPGGLSVAA TGLAGS
//
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