ID F3LIP7_9GAMM Unreviewed; 341 AA.
AC F3LIP7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=IMCC1989_1491 {ECO:0000313|EMBL:EGG93240.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG93240.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG93240.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG93240.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(2011).
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:EGG93240.1}.
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DR EMBL; AEVK01000242; EGG93240.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LIP7; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000010300; Unassembled WGS sequence.
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; 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 SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:EGG93240.1};
KW Cilium {ECO:0000313|EMBL:EGG93240.1};
KW Flagellum {ECO:0000313|EMBL:EGG93240.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGG93240.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000010300}.
FT DOMAIN 180..338
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 112..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 38159 MW; 0A2FC8D5372DA205 CRC64;
MNNTMQYDVS KLTAQQSYTD LASLQNIKKD GRENQDLALR QVAQQFESMF VQMMLKSMRS
ANEVFGQDNP LNSSEMKHHQ EMYDNQLSLS LSASNKIGLA DAFYRQMKSN YVSSETPTET
NASNEGVSDI SRRNTSVDNA IYQSMLSKMP TPESIAPSNN ATNSIFSQPL NVSKQSVQDD
VALNNIESPE DFIQMLTPYA KKAAAILGVD YQVLIAQSAL ETGWGKHVIK DGYGKQSFNL
FNIKADSRWE GKAVNVPTIE YVNGVANKEV ASFRRYDSIE ESVNDYLQFL TQPRYEKALA
STNSSDFIHG LQNAGYATDP RYADKIQRII DTALPKKSTQ N
//
