ID A0A432ZJA8_9GAMM Unreviewed; 311 AA.
AC A0A432ZJA8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=CWI81_00590 {ECO:0000313|EMBL:RUO78097.1};
OS Idiomarina seosinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=281739 {ECO:0000313|EMBL:RUO78097.1, ECO:0000313|Proteomes:UP000287908};
RN [1] {ECO:0000313|EMBL:RUO78097.1, ECO:0000313|Proteomes:UP000287908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-SP19 {ECO:0000313|EMBL:RUO78097.1,
RC ECO:0000313|Proteomes:UP000287908};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO78097.1}.
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DR EMBL; PIQF01000001; RUO78097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZJA8; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000287908; 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; 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:RUO78097.1};
KW Cilium {ECO:0000313|EMBL:RUO78097.1};
KW Flagellum {ECO:0000313|EMBL:RUO78097.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RUO78097.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000287908}.
FT DOMAIN 156..311
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 311 AA; 34270 MW; 74FE1B98061CDCF2 CRC64;
MFELASQRQA TSAMDTHALD GLRKQAFGDN KEAALREAAE QFEAIFLNMV LGSMRKANDV
FAKDNPLNSR YTQMYRDMHD QQLTSELSSQ GSLGLADMMV KQLSGQAGLD KSERFGANLG
EAKMPVNKPE VSDQGGIDAG LYYGGKRVNQ VRLDEGEARF QSPQDFIAAI KPQAEKIAAE
SGIDANVLVA QAALETGWGQ RIIPGRHGGS SNNLFNIKAD QRWGGDQSHV STLEFDGNVA
KKERAAFRSY QNVEQSLQDY VDFIKGHPRY QQALQVADDP KQYAEQLQQA GYATDPQYAA
KIQAVMNKIA K
//
