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Database: UniProt
Entry: A0A0M2Q049_PROHO
LinkDB: A0A0M2Q049_PROHO
Original site: A0A0M2Q049_PROHO 
ID   A0A0M2Q049_PROHO        Unreviewed;       539 AA.
AC   A0A0M2Q049;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Cell wall hydrolase {ECO:0000313|EMBL:KKJ00017.1};
GN   ORFNames=PROH_09585 {ECO:0000313|EMBL:KKJ00017.1};
OS   Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC   Prochlorotrichaceae; Prochlorothrix.
OX   NCBI_TaxID=317619 {ECO:0000313|EMBL:KKJ00017.1, ECO:0000313|Proteomes:UP000034681};
RN   [1] {ECO:0000313|EMBL:KKJ00017.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ00017.1};
RA   Shanker A., Yadav P., Khan S., Sharma V.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKJ00017.1, ECO:0000313|Proteomes:UP000034681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CALU 1027 {ECO:0000313|EMBL:KKJ00017.1};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKJ00017.1}.
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DR   EMBL; AJTX02000004; KKJ00017.1; -; Genomic_DNA.
DR   RefSeq; WP_017711321.1; NZ_KB235933.1.
DR   AlphaFoldDB; A0A0M2Q049; -.
DR   STRING; 317619.GCA_000332315_00675; -.
DR   eggNOG; COG0860; Bacteria.
DR   Proteomes; UP000034681; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR022222; DUF3747.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF12565; DUF3747; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KKJ00017.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034681}.
FT   DOMAIN          420..529
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          226..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..352
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  58073 MW;  C28BF504E7100E9E CRC64;
     MITALLRSSI RRAAVLRRGL LHRLTPMALV TATALTATLG GLSAPALALS EFGQQELDQS
     RTIAVAKPVD NGRFYQLLIL RQVSNQRACW QELPGQPTRI DPLLLNFDFT GICDRSVDSN
     GYSVRLAGED LNWQYRLQLV KQGGQLVLQA VSAANRAAPP LTIGRTNGLG EGFLKVSLDP
     GWRLTQRLYN GQPLGHVYVT HDQSLAALAG VPSAPVPPPV TTPPIVATPP RQPVPQPNPL
     PPVVVPSPPT LPGPPSGNPG AATNYRVIVP NTSADTQRRV QAVEPGAFRT TLNGQSVIQA
     GLFQEQWRAI ELQQNLMAAR IPAQIIQGTG VVPPRPNPPL PNPQSPNPLP PTQIPVGRIR
     VILDPGHGGR DPGAVGIGGL QEKEINLDIA RRVQQILESR GIAVMLTRPG DVEVELEPRV
     DQAERMAAQL FVSIHANAIS MDRPEVNGLE TYYYDSGSGL AQTIHNSILR GTDLRDRGVR
     QARFYVLRNT SMPSVLVETG FVTGSEDAAR FRNSEARGQI AQAIAQGILT YAQQTALAP
//
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