ID A8H288_SHEPA Unreviewed; 363 AA.
AC A8H288;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN OrderedLocusNames=Spea_1348 {ECO:0000313|EMBL:ABV86675.1};
OS Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV86675.1, ECO:0000313|Proteomes:UP000002608};
RN [1] {ECO:0000313|EMBL:ABV86675.1, ECO:0000313|Proteomes:UP000002608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT "Complete sequence of Shewanella pealeana ATCC 700345.";
RL Submitted (OCT-2007) 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}.
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DR EMBL; CP000851; ABV86675.1; -; Genomic_DNA.
DR RefSeq; WP_012154601.1; NC_009901.1.
DR AlphaFoldDB; A8H288; -.
DR STRING; 398579.Spea_1348; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR KEGG; spl:Spea_1348; -.
DR eggNOG; COG1705; Bacteria.
DR eggNOG; COG3951; Bacteria.
DR HOGENOM; CLU_013771_3_0_6; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000002608; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.70.40; peptidoglycan hydrolase; 1.
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 NCBIfam; TIGR02541; flagell_FlgJ; 1.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:ABV86675.1};
KW Cilium {ECO:0000313|EMBL:ABV86675.1};
KW Flagellum {ECO:0000313|EMBL:ABV86675.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000002608}.
FT DOMAIN 196..355
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 141..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 39790 MW; 27EBD7F74F14299F CRC64;
MEKLSNASQF LDLGGLDSLR SRAQKDETSA LKEVAQQFEG IFVQMLMKSM RDANAVFESD
SPMNSQYTKF YEQMHDQQMS LNLSGEGMLG LADLMVQQLD PANSPMTPAS VLRGDINGGS
KAAALTMDRP DMLQMPSSRI ASPDTITDHV PKNQNSFASN SQASAPQAIT SSVQSQTLDS
VLSGKILPSA AVNADKSQAN FTSQDEFVAR LYPHAQKAAQ TLGTTPEVLI AQSALETGWG
QKMVKGHQGQ QSNNLFNIKA DNRWQGEKAS VSTLEYEQGI AVKQQANFRV YEDIGQSFND
FVSFVSNGER YQDAMKQAAN PQAFIRSLQE AGYATDPKYA DKVIQVMKTI TRDFKDVLQG
VKQ
//
