ID A0A1H3YKS1_9GAMM Unreviewed; 356 AA.
AC A0A1H3YKS1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=SAMN02745729_101500 {ECO:0000313|EMBL:SEA11552.1};
OS Marinobacterium iners DSM 11526.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1122198 {ECO:0000313|EMBL:SEA11552.1, ECO:0000313|Proteomes:UP000242469};
RN [1] {ECO:0000313|Proteomes:UP000242469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11526 {ECO:0000313|Proteomes:UP000242469};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNRJ01000001; SEA11552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3YKS1; -.
DR STRING; 1122198.SAMN02745729_101500; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000242469; 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 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:SEA11552.1};
KW Cilium {ECO:0000313|EMBL:SEA11552.1};
KW Flagellum {ECO:0000313|EMBL:SEA11552.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000242469}.
FT DOMAIN 182..350
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 134..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39059 MW; 9F8B230E5912515E CRC64;
MAIDSGRLTP SQAALFTDLN QLQKLKTQAG NDQQAALQGV AQEFEQLFMN MMLKSMRQAS
DVLASDSPFN SGDVKFYQEM FDQQLTLDLS KKDSIGLADI IVKQLSQQHA PVVAPGQDEE
KGDQQSMTEQ MLSRAFGGGP LPQAPAGNYR APSASESEQE GNSDMVQPVA QELTDQDKAD
SETAAVKETL PARFETPAEF IEKLMPLAEQ AGKELGVNPN VLLAQAALET GWGKFITRDA
TSGESSRNLF NIKAHRGWEG DTAKVQTLEY RGGVPEKEQA RFRAYDSYAD SFSDYVDFLR
SNPRYQQALE QGADPTRFVR ELHNAGYATD PEYANKIERI FSGDLLAGLG RGAKEG
//
