ID A0A2R7SG70_9BURK Unreviewed; 288 AA. AC A0A2R7SG70; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 12-AUG-2020, entry version 9. DE RecName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00016309}; DE AltName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433}; GN Name=flgJ {ECO:0000313|EMBL:PTT81973.1}; GN ORFNames=DBR42_17345 {ECO:0000313|EMBL:PTT81973.1}; OS Pelomonas sp. HMWF004. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Pelomonas; unclassified Pelomonas. OX NCBI_TaxID=2056841 {ECO:0000313|EMBL:PTT81973.1, ECO:0000313|Proteomes:UP000244686}; RN [1] {ECO:0000313|Proteomes:UP000244686} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMWF004 {ECO:0000313|Proteomes:UP000244686}; RA Muscarella M.E.; RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the CC peptidoglycan layer to assemble the rod structure in the periplasmic CC space. {ECO:0000256|ARBA:ARBA00002954}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl CC hydrolase 73 family. {ECO:0000256|ARBA:ARBA00007974}. CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family. CC {ECO:0000256|ARBA:ARBA00006880}. 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:PTT81973.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; QAJF01000932; PTT81973.1; -; Genomic_DNA. DR Proteomes; UP000244686; Unassembled WGS sequence. DR GO; GO:0004040; F:amidase activity; IEA:InterPro. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro. DR InterPro; IPR019301; Flagellar_prot_FlgJ_N. DR InterPro; IPR013377; FlaJ. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom. DR Pfam; PF01832; Glucosaminidase; 1. DR Pfam; PF10135; Rod-binding; 1. DR SMART; SM00047; LYZ2; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR TIGRFAMs; TIGR02541; flagell_FlgJ; 1. PE 3: Inferred from homology; KW Cell projection {ECO:0000313|EMBL:PTT81973.1}; KW Cilium {ECO:0000313|EMBL:PTT81973.1}; KW Flagellum {ECO:0000313|EMBL:PTT81973.1}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000313|EMBL:PTT81973.1}; KW Periplasm {ECO:0000256|ARBA:ARBA00022764}; KW Reference proteome {ECO:0000313|Proteomes:UP000244686}. FT DOMAIN 125..281 FT /note="LYZ2" FT /evidence="ECO:0000259|SMART:SM00047" SQ SEQUENCE 288 AA; 30562 MW; FF4A03A738711EF8 CRC64; MSSFQSISGQ SLGSVEALKA SAARDPKGSI REAAKQFESL FMQEVMKSMR ASTLSSGMLD NNATQLGTEM LDTQFAGKMS GLPGGLSEAI QRQLQRQMGM QDLSPENIKK ASQTTLAQAL PALATKGIPN HVQSFIQQHD ASARAASAAT GIPASFMVAQ AAHESGWGKR EITGADGSKS HNIFGIKATP GWTGKTVDVR TTEVINGQAV KVTAKFRAYG SYDEAFKDYA RLISSNDRYA KVVAEAQTGN AAGFARGLQQ AGYATDPAYA EKLARTITTT QRVQSTLA //